MXPA00000033A - Receptor kinase, bin1 - Google Patents

Abstract

A novel plant steroid receptor, Bin1, is provided, as well as polynucleotides encoding Bin1. Bin1 polypeptide is useful in promoting increased plant yield and/or increased plant biomass. Genetically modified plants characterized as having increased yield and methods for producing such plants are also provided.

Description

RECEIVER OUINASE BINl This invention was made with governmental support in the United States, under grant No. DIR 9116923, granted by the National Science Foundation, and concession No. 93-373019125, granted by the United States Department of Agriculture. The government of the United States has certain rights in this invention. Field of the Invention The present invention relates in general to plant genetic engineering, and specifically to a novel gene useful for producing genetically engineered vegetables characterized by having an increased crop yield phenotype, increased disease resistance, and a vegetative growth phase. of longer duration. BACKGROUND OF THE INVENTION Brassinosteroids are an exclusive class of biologically active natural products that possess plant steroid hormone activity. Their effective low concentrations for use in crops make them environmentally safe and the brassinosteroids used on a large scale are generally non-toxic. Physiologically, brassinosteroids produce many changes and could represent a new class of hormones in vegetables. The economic aspects of brassinosteroids can have global effects. For example, brassinosteroids can be used as vegetable protectants both in the adversity of pesticides and in the environment. In addition, brassinosteroids appear to be useful for insect control. In addition, brassinosteroids can regulate some stages of the reproductive cycle in plants, thereby providing the means to increase or decrease the reproductive process. For example, in certain vegetable crops, it may be desirable to eliminate the flowering process to ensure the continuous production of other tissues such as leaves, bulbs and other storage organs. This modulation of the reproductive process can be important in the control of certain seeds that have bad weeds, where the cessation of the flowering cycle eliminates future generations. The brassinosteroids also seem to stimulate the growth of the roots, and the external application does not cause deformity to the plants. Brassinosteroids qualify for classification as biochemical pesticides. These pesticides are generally distinguished from conventional chemical pesticides by their exclusive modes of action, low effective concentration, target species, and specificity. Historically, brassinosteroids have not been used in real agricultural applications due to the expense involved in producing them as well as the difficulty in purifying them. It is known that as soon as hormones, such as glucocorticoids, enter a cell, they bind to specific receptor proteins, thereby creating a ligand / receptor complex. The binding of the hormone to the receptor is thought to initiate an allosteric alteration of the receptor protein. As a result, it is believed that the ligand / receptor complex is able to bind with high affinity to certain specific sites in the chromatin nucleic acid. These sites, which are known as response elements, modulate the expression of nearby target gene promoters. Recent evidence indicates that in addition to intracellular, genomic effects, steroids also exhibit non-genomic effects, that is, they affect the surface of cells and alter the permeability of ions, as well as release neurohormones and neurotransmitters. Steroids such as estrogens and adrenal steroids and their naturally occurring and synthetic analogs have shown effects on the membrane. In view of the above, it appears that steroids can cause synergistic interactions between non-genomic and genomic responses resulting in alterations in neural activity or in certain aspects of oocyte and sperm maturation, for example. Compendium of the invention Although steroid hormones are important for the development of animals, the physiological role of plant steroids is very unknown. The present invention is based on the discovery of the Binl gene, which encodes a polypeptide that functions as a receptor kinase and is involved in the response path of brasinolide. In a first embodiment, the invention provides Binl polypeptide that binds to brassinosteroids and isolated polynucleotide sequences that encode Binl. In another embodiment, the invention provides a method for producing a genetically modified plant characterized by having an increased yield as compared to a natural type plant. The method is based on introducing at least one nucleic acid sequence encoding the Bin1 polypeptide, operably associated with a promoter, to a plant cell to obtain a transformed plant cell and produce a plant from the transformed plant cell. These genetically modified vegetables may exhibit increased crop yield or increased biomass. In yet another embodiment, the invention provides a method for producing a plant characterized by having increased yield by contacting a plant that has a natural gene binl operably linked to its natural promoter, with an amount that induces the promoter of an inducing agent. the expression of the binl gene, wherein the elevation of the expression of the binl gene results in the production of a plant that has an increased yield as compared to a plant that has not been put in contact with the induction agent. Thus, transcription factors or chemical agents can be used to increase the expression of Binl in a plant, in order to provide increased yield. Alternatively, plants genetically transformed with Binl can also be contacted with an amount that induces the promoter of an agent that elevates the expression of Binl to obtain plants that have increased yield. Brief Description of the Drawings Figures 1A-C show the nucleotide sequences (A, B) and deduced amino acids (C) of Binl of the invention (SEQ ID NO: 1 and SEQ ID NO: 2, respectively). DESCRIPTION OF THE PREFERRED EMBODIMENTS The present invention provides a novel steroid receptor kinase, Binl, which is involved in the pathway for the synthesis of the plant steroid hormone, brasinolide. The over-expression of Binl in transgenic plants provides vegetables characterized by having an increased resistance to the disease, increased yield of the vegetable or vegetative biomass and increased seed yield. As used herein, the term "yield" or "increased plant yield" refers to increasing the plant biomass or the yield of the seeds in relation to the wild-type biomass. POLYPEPTIDES AND POLYCELLOTES B ± nl In a first embodiment, the present invention provides the substantially pure Binl polypeptide. Binl polypeptide is exemplified by the amino acid sequence shown in Figure 1 and SEQ ID NO: 2. Binl polypeptide is characterized as having a predicted molecular weight of 130 kDa as determined by SDS-PAGE, and because it functions in the response path of the brasinolide. The term "substantially pure" as used herein refers to the Bin1 polypeptide that is substantially free of other proteins, lipids, carbohydrates or other materials with which it naturally associates. A person skilled in the art can purify Binl using standard techniques for the purification of proteins. The substantially pure polypeptide will yield a single band greater than about 130 kDa on a denatured polyacrylamide gel. The purity of the Binl polypeptide can also be determined by analysis of amino-terminal amino acid sequences. The invention includes a functional Binl polypeptide as well as functional fragments thereof. As used in this, the term "functional polypeptide" refers to a polypeptide that possesses biological function or activity that is identified through a defined functional assay and which is associated with a particular biological, morphological, or phenotypic alteration in the cell. The term "functional fragments of the Binl polypeptide" refers to all Binl fragments that retain the activity of Binl, for example, the receptor kinase activity of the protein or the ability to bind brassinosteroids. Biologically functional fragments, for example, can vary in size from a polypeptide fragment as small as an epitope capable of binding an antibody molecule to a large polypeptide capable of participating in the characteristic induction or programming of phenotypic changes within a cell. An example of a functional fragment of Binl is a polypeptide that includes the amino acid residue from about 588 to 649 of SEQ ID NO: 2. This fragment includes the binding domain of brassinosteroids of the Bin1 polypeptide. Another functional fragment of Binl is a polypeptide that includes the amino acid residue from about 831 to 1196 of SEQ ID NO: 2. This fragment includes the domain of the protein kinase of the Binl polypeptide. The receptor activity of the Binl protein kinase and the role of Binl in the response path of brasinolide can be used in biological assays to identify biologically active fragments of the Binl polypeptide or related polypeptides. For example, Binl can not only bind brassinosteroids, but also other hormones, therefore a test can be performed to detect Binl binding activity. In addition, Binl inhibitors can be used to cause loss of Binl function resulting in, for example, male sterile plants, short stature, reduced yield, and so on. Furthermore, inhibition of Binl can be useful in horticulture to create dwarf varieties. Minor modifications of the amino acid sequence of Binl can result in proteins having substantially equivalent activity to the Binl polypeptide described herein in SEQ ID NO: 2 (Figure 1). These modifications can be deliberate, such as by site-directed mutagenesis, or they can be spontaneous. All of the polypeptides produced by those modifications of Binl are included herein as long as the peptide possesses the biological activity of Binl (ie, receptor activity of the protein kinase). In addition, the deletion of one or more amino acids can also result in a modification of the structure of the resulting molecule without significantly altering its activity. The suppression can lead to the development of a smaller active molecule which could have wider utility. For example, it may be possible to remove amino or carboxy terminal amino acids required for Binl activity. For example, a less active form of Binl has an amino acid change at residue 611 from glycine to glutamic acid. This mutant form has reduced affinity for the steroid. Other mutants can be produced that activate the enzymatic activity. For example, a mutant can be produced in a manner that expresses the kinase domain, thereby allowing the constitutive activity of the kinase.

The Binl polypeptide includes amino acid sequences substantially the same as the sequence presented in SEQ ID NO: 2. The term "substantially the same" refers to the amino acid sequences that retain the activity of Binl as described herein, for example, the receptor activity of the protein kinase. The Binl polypeptides of the invention include conservative variations of the polypeptide sequence. The term "conservative variation" as used herein denotes the replacement of an amino acid residue by another biologically similar residue. Examples of conservative variations include the substitution of a hydrophobic residue such as isoleucine, valine, leucine or methionine for another, or the substitution of one polar residue for another, such as the substitution of arginine for lysine, glutamic acid for aspartic acid, or glutamine for asparagine, and the like. The term "conservative variation" also includes the use of a substituted amino acid in place of an unsubstituted parent amino acid provided that the antibodies raised from the substituted polypeptide also react immunologically with the unsubstituted polypeptide. In another aspect, the invention provides isolated polynucleotides encoding the Binl polypeptide having the amino acid sequence presented in SEQ ID NO: 2. The Binl gene has been mapped at a 5 kb interval on chromosome 4 of Arabidopsis. The Binl transcript contains a single, long open reading frame that encodes a protein of 1196 amino acids. The term "isolated" as used herein includes polynucleotides substantially free of other nucleic acids, proteins, lipids, carbohydrates or other materials with which it is naturally associated. The polynucleotide sequences of the invention include nucleic acid, cDNA and RNA sequences encoding Binl. It is understood that polynucleotides that encode all or the variant portions of Binl are included herein, as long as they encode a polypeptide with Binl activity. These polynucleotides include naturally occurring, synthetic, and intentionally manipulated polynucleotides as well as manipulated variants. For example, portions of the mRNA sequence can be altered due to alternative RNA overlap patterns or the use of alternating promoters for RNA transcription. Furthermore, the Binl polynucleotides of the invention include polynucleotides that have alterations in the nucleic acid sequence that still encode functional Binl. Alterations of the nucleic acid include but are not limited to intragenic mutations (eg, point mutation, nonsense (stop), anti-sense, overlapped site and frame change) and heterozygous or homozygous deletions. Detection of these alterations can be done by standard methods known to those skilled in the art including sequence analysis, Southern spotting analysis, polymerase chain reaction based assays (e.g., multiplex polymerase chain reaction, tagged sites in sequence (STS)) and hybridization at the site. The polynucleotide sequences of the invention also include anti-sense sequences. The polynucleotides of the invention include sequences that degenerate as a result of the genetic code. There are 20 natural amino acids, most of which are specified by more than one codon. Therefore, all degenerate nucleotide sequences are included in the invention as long as the amino acid sequence of the Bin1 polypeptide encoded by these nucleotide sequences retains the receptor activity of the Bin1 protein kinase. A "functional polynucleotide" denotes a polynucleotide that encodes a functional polypeptide as described herein. In addition, the invention also includes a polynucleotide that encodes a polypeptide having a biological activity of the amino acid sequence presented in SEQ ID NO: 2 and having at least one epitope for an antibody immunoreactive with the Binl polypeptide. As used in this, the terms polynucleotide and nucleic acid sequences of the invention refer to nucleic acid, RNA and cDNA sequences. The polynucleotides encoding Binl include the nucleotide sequence presented in Figure 1 (SEQ ID NO: 1), as well as nucleic acid sequences complementary to this sequence. The complementary sequences may include anti-sense polynucleotides. When the sequence is RNA, deoxyribonucleotides A, G, C and T of Figure 1C are replaced by ribonucleotides A, G, C, and U, respectively. Also included in the invention are fragments ("probes") of the aforementioned nucleic acid sequences that are at least 15 bases in length, which is sufficient to allow the probe to selectively hybridize to the nucleic acid encoding the amino acid sequence presented in Figure 1 (SEQ ID NO: 2). "Selective hybridization" as used herein refers to hybridization under moderately stringent or very stringent physiological conditions (see, for example, the techniques described in Maniatis et al., 1989 Molecular Cloning A Laboratory Manual, Cold Spring Harbor Laboratory, NY, incorporated herein by reference), which distinguishes related nucleotide sequences from those not related to Binl. Specifically, a cDNA sequence for Binl is described herein. Figure 1 shows the complete cDNA and the deduced protein sequences (SEQ ID NOs: 1 and 2, respectively). It is understood that homologues of the plant Binl are included herein and can be identified, for example, using binl nucleic acid probes from plant based on SEQ ID NO: 1. In the nucleic acid hybridization reactions, the conditions used for achieving a particular level of rigor will vary, depending on the nature of the nucleic acids that are being hybridized. For example, the length, degree of complementarity, the composition of nucleotide sequences (e.g., GC v. AT content), and the type of nucleic acid (e.g., RNA v. Nucleic acid) of the hybridizing regions can be Consider when selecting the hybridization conditions. A further consideration is whether one of the nucleic acids is immobilized, for example, on a filter. As an example of conditions of progressively greater rigor is the following: 2 x SSC / 0.1% SDS at approximately room temperature (hybridization conditions); 0.2 x SSC / 0.1% SDS at approximately room temperature (low stringency conditions), 0.2 x SSC / 0.1% SDS at approximately 42 ° C (conditions of moderate rigor); and 0.1 x SSC at approximately 68 ° C (high stringency conditions). The washing can be carried out using only one of these conditions, for example, high stringency conditions, or each of the conditions can be used, for example, for 10 to 15 minutes each, in the order listed above, repeating any or all of the steps listed. The optimal conditions may vary depending on the particular hybridization reaction involved, and can be determined empirically. The nucleic acid sequences of the invention can be obtained by various methods. For example, the nucleic acid can be isolated using hybridization or computer-based techniques that are well known in the art. These techniques include, but are not limited to: 1) hybridization of genomic or cDNA libraries with probes to detect homologous nucleotide sequences; 2) selection of antibodies from expression libraries to detect fragments of cloned nucleic acids with shared structural characteristics; 3) polymerase chain reaction (PCR) in genomic nucleic acid or cDNA using primers capable of annealing to the nucleic acid sequence of interest; 4) computer searches of sequence databases to find similar sequences; and 5) differential selection of subtracted nucleic acid library. Selection procedures that rely on nucleic acid hybridization make it possible to isolate any gene sequence from any organism, provided that the appropriate probe is available. Oligonucleotide probes, which correspond to a part of the Binl sequence encoding the protein in question, can be chemically synthesized. This requires that stretches of short oligopeptides of the amino acid sequence must be known. The sequence of nucleic acids encoding the protein can be deduced from the genetic code, however, the degeneracy of the code must be taken into account. It is possible to perform a mixed addition reaction when the sequence is degenerate. This includes a heterogeneous mixture of denatured double stranded nucleic acid. For this selection, hybridization is preferably performed either on the single-stranded nucleic acid or on denatured double-stranded nucleic acid. Hybridization is particularly useful in the detection of cDNA clones derived from sources where an extremely low amount of mRNA sequences related to the polypeptide of interest is present. In other words, using stringent hybridization conditions directed to avoid non-specific binding, it is possible, for example, to allow autoradiographic visualization of a specific cDNA clone by hybridizing the target nucleic acid to a single probe in the mixture which it is its complete complement (Wallace, et al., Nucí, Acid Res., 9: 879, 1981). Alternatively, a subtractive library, as illustrated herein is useful for the removal of nonspecific cDNA clones. When the amino acid sequence is not known, direct synthesis of nucleic acid sequences is not possible and the synthesis of cDNA sequences is the method of choice. Among standard procedures for isolating the cDNA sequence of interest is the formation of cDNA libraries carrying plasmids or phages that are derived from the reverse transcription of mRNA which is abundant in donor cells that have a high level of gene expression. When used in combination with polymerase chain reaction technology, even rare expression products can be cloned. In cases where significant portions of amino acid sequences of a polypeptide are known, the production of single or double-stranded RNA nucleic acid probes sequences can be employed by duplicating a sequence putatively present in the target cDNA in acid hybridization procedures nucleic acid / nucleic acid that are carried out on cloned copies of the cDNA that have been denatured in single chain form (Jay, and collaborators, Nucí. Acid Res. , 1.1: 2325, 1983). A cDNA expression library, such as lambda gtll, can be selected indirectly from Binl peptides using antibodies specific for Binl. These antibodies can be polyclonal or monoclonal and used to detect the product of the indicator expression of the presence of Binl cDNA. The detection of alterations in Binl nucleic acid (eg, point mutation, nonsense (stop), missense, overlap site and change of frame) and heterozygous or homozygous deletions can be effected by standard methods known to those skilled in the art. techniques that include sequence analysis, Southern spotting analysis, polymerase chain reaction based assays (e.g., multiplex polymerase chain reaction, sequence tagged sites (STS)) and site hybridization. These proteins can be analyzed by standard SDS-PAGE and / or immunoprecipitation analysis and / or Western blot analysis, for example. The nucleic acid sequences encoding Binl can be expressed in vitro by transfer of nucleic acid into a convenient host cell. "Host cells" are cells in which a vector can be propagated and its nucleic acid expressed. The term "host cells" also includes any progeny or graft material, for example, from the parent host cell. It is understood that all progeny may not be identical to the parent cell as there may be mutations that occur during replication. However, this progeny is included when the term "host cell" is used. Stable transfer methods are known in the art, which means that the foreign nucleic acid is continuously maintained in the host. In the present invention, Binl polynucleotide sequences can be inserted into a recombinant expression vector. The terms "recombinant expression vector" or "expression vector" refer to a plasmid, virus or other vehicle known in the art that has been manipulated by the insertion or incorporation of the Binl genetic sequence. These expression vectors contain a promoter sequence that facilitates efficient transcription of the inserted Binl sequence. The expression vector typically contains a replication origin, a promoter, as well as specific genes that allow phenotypic selection of the transformed cells. Methods that are well known to those skilled in the art can be used to construct expression vectors containing the Bin1 coding sequence and suitable transcription / translation control signals. These methods include recombinant nucleic acid techniques in vi tro, synthetic techniques, and in vivo recombination / genetics techniques (see, for example, the techniques described in Maniatis et al., 1989 Molecular Cloning A Laboratory Manual, Cold Spring Harbor Laboratory, NY ). A variety of host expression vector systems can be used to express the Binl coding sequence. These include but are not limited to microorganisms such as bacteria transformed with expression vectors of recombinant bacteriophage nucleic acid, plasmid nucleic acid or cosmid nucleic acid containing the coding sequence Binl.; the yeast transformed with recombinant yeast expression vectors containing the Binl coding sequence; plant cell systems infected with recombinant virus expression vectors (e.g., cauliflower mosaic virus, CaMV, tobacco mosaic virus, TMV) or transformed with recombinant plasmid expression vectors (e.g., Ti plasmid) contains the Binl coding sequence; insect cell systems infected with recombinant virus expression vectors (e.g., baculovirus) that contain the Binl coding sequence; or system of cells from animals infected with recombinant virus expression vectors (e.g., retroviruses, adenoviruses, vaccinia viruses) that contain the Binl coding sequence, or overlapping transformed animal cell systems for stable expression. Depending on the host / vector system used, any of several convenient elements of transcription and translation, including constitutive and inducible promoters, transcription enhancer elements, transcription terminators, etc. can be used in the expression vector (see for example, Bitter and collaborators, 1987, Methods in Enzymology 153: 516-544). For example, when bacterial systems are cloned, inducible promoters such as pL of bacteriophage Y, plac, ptrp, ptac (ptrp-lac hybrid promoter) and the like can be used. When cloning into mammalian systems, promoters derived from the genome of mammalian cells (eg, the metallothionein promoter) or mammalian viruses (eg, the long terminal repeat of retroviruses, the latter promoter of adenovirus, the promoter of 7.5 K of vaccine viruses) can be used. Promoters produced by recombinant nucleic acid or by synthetic techniques can also be used to provide the transcription of inserted Binl coding sequences. In yeast, several vectors containing constitutive or inducible promoters can be used. For a review see, Current Protocols in Molecular Biology, Vol. 2, 1988, Ed. Ausubel et al., Greene Publish. Assoc. & Wiley Inters-cience, Ch. 13; Grant et al., 1987, Expression and Secretion Vectors for Yeast, in Methods in Enzymology, Eds. Wu & Grossman, 31987, Acad. Press, N.Y., Vol. 153, pp. 516-544; Glover, 1986, DNA Cloning, Vol. II, IRL Press, Wash., D.C., Ch. 3; and Bitter, 1987, Heterologous Gene Expression in Yeast, Methods in Enzymology, Eds. Berger & Kimmel, Acad. Press, N.Y., Vol. 152, pp. 673-684; and The Molecular Biology of the Yeast Saccharomyces, 1982, Eds. Strathern et al., Cold Spring Harbor Press, Vols. I and II. A constitutive yeast promoter such as ADH or LEU2 or an inducible promoter such as GAL can be used (cloning in yeast, Chapter 3, R. Rothstein In: DNA Cloning Vol. 11, A Practical Approach, Ed. DM Glover, 1986, IRL Press, Wash., DC). Alternatively, vectors that promote the integration of foreign nucleic acid sequences into the yeast chromosome can be used. Eukaryotic systems, and preferably mammalian expression systems, allow suitable post-translational modifications of expressed mammalian proteins. Eukaryotic cells possessing the cellular machinery for proper processing of the primary transcript, glycosylation, phosphorylation, and advantageously, the plasma membrane insertion of the gene product can be used as host cells for the expression of Binl. Mammalian expression systems that use recombinant viruses or viral elements to direct expression can overlap. For example, when adenovirus expression vectors are used, the Binl coding sequence can be ligated to an adenovirus transcription / translation control complex, eg, the last promoter and the tripartite forward sequence. Alternatively, the 7.5K promoter of the vaccinia virus can be used. (For example, see, Mackett et al., 1982, Proc. Nati, Acad. Sci. USA 79: 7415-7419; Mackett et al., 1984, J. Virol. 49: 857-864; Panicali et al., 1982, Proc. Nati Acad. Sci. USA 79: 4927-4931). Of particular interest are vectors based on bovine papilloma virus which have the ability to replicate as extrachromosomal elements (Sarver et al., 1981, Mol.Cell. Biol. 1: 486). Shortly after the entry of its nucleic acid into mouse cells, the plasmid replicates at approximately 100 to 200 copies per cell. Transcription of inserted cDNA does not require integration of the plasmid into the host chromosome, thereby producing a high level of expression. These vectors can be used for stable expression including a selectable marker in the plasmid, such as, for example, the neo gene. Alternatively, the retroviral genome can be modified for use as a vector capable of introducing and directing the expression of the Binl gene in host cells (Cone &Mulligan, 1984, Proc. Nati, Acad. Sci. USA 81: 6349-6353) . High level expression can also be achieved using inducible promoters, including, but not limited to, the metallothionein IIA promoter and heat shock promoters. For the long-term, high-yield production of recombinant proteins, stable expression is preferred. Instead of using expression vectors containing viral replication origins, the host cells can be transformed with Binl cDNAs controlled by suitable expression control elements (e.g., promoter, enhancer, sequences, transcription terminators, polyadenylation sites, etcetera), and a selectable marker. The selectable marker in the recombinant plasmid confers resistance to selection and allows the cells to stably integrate the plasmid into their chromosomes and grow to form foci which in turn can be cloned and expanded into cell lines. For example, after the introduction of foreign nucleic acid, the overlapping cells can be allowed to grow for one or two days in an enriched medium, and then they are changed to a selective medium. Various selection systems can be used, including, but not limited to: the thymidine kinase gene of herpes simplex virus (Wigler et al., 1977, Cell IX-223), the hypoxanthine-guanine phosphoribosyltransferase gene (Szybalska & Szybalski, 1962, Proc. Na ti. Acad. Sci. USA 48: 2026), and that of adenine phosphoribosyltransferase (Lo et al., 1980, Cell 22: 817) can be used in tk-, hgprt or aprt cells respectively. Additionally, antimetabolite resistance can be used as the basis of selection for dhfr, which confers resistance to methotrexate (Wigler et al. 1980, Nati. Acad. Sci. USA 77: 3567; O'Hare and collaborators, 1981, Proc. Na ti. Acad. Sci. USA 78.:1527); the gpt gene, which confers resistance to mycophenolic acid (Mulligan &Berg, 1981, Proc. Na ti.Acid. Sci. USA 7.8: 2072); the neo gene, which confers resistance to aminoglycoside G-418 (Colberre-Garapin et al., 1981, J. Mol. Biol. 150: 1); and hygro gene, which confers resistance to hygromycin (Santerre et al., 1984, Gene 30: 147). Recently, additional selectable genes have been described, namely trpB, which allows cells to use indole instead of tryptophan; hisD, which allows cells to use histinol in place of histidine (Hartman &Mulligan, 1988, Proc.Nat.Acid.Sci.USA 85: 8047); and ODC (ornithine decarboxylase) that confers resistance to the ornithine decarboxylase inhibitor, 2- (difluoromethyl) -DL-ornithine, DFMO (McConlogue L., 1987, In: Current Communications in Molecular Biology, Cold Spring Harbor Laboratory ed.). When the host is eukaryotic, the nucleic acid transaction can be carried out using calcium phosphate coprecipitates and conventional mechanical methods such as microinjection, electroporation, insertion of a plasmid embedded in liposomes, or virus vectors. Eukaryotic cells can also be cotransformed with a nucleic acid sequence encoding a Binl polypeptide of the invention, and a second foreign nucleic acid molecule encoding a selectable phenotype. Another method employs a eukaryotic viral vector, such as simian virus 40 (SV40) or bovine papilloma virus, to transiently infect or transform eukaryotic cells and express the protein. (See, for example, Eukaryotic Viral Vectors, Cold Spring Harbor Laboratory, Gluzman ed., 1982). The isolation and purification of recombinantly expressed polypeptides, or fragments thereof, provided by the invention, can be carried out by conventional elements including preparative chromatography and immunological separations involving monoclonal or polyclonal antibodies. BIN1 ANTIBODIES The invention also includes immunoreactive antibodies with Binl polypeptide or antigenic fragments thereof. The antibodies of the invention are useful for modulating Binl ligand bonds, for example. Antibodies directed against peptides derived from the extracellular domain of Binl (for example, peptides contained in the domain of about amino acid 588 to 649 of SEQ ID NO: 2) are preferred. The antibody is provided consisting essentially of monoclonal antibodies raised with different epitopic specificities, as well as different monoclonal antibody preparations. Monoclonal antibodies are made of antigens that contain fragments of the protein by methods well known to those skilled in the art (Kohier, et al., Na ture, 256: 495, 1975). The preparation of polyclonal antibodies is well known to those skilled in the art. See, for example, Green et al., Production of Polyclonal Antisera, in IMMUNOCHEMICAL PROTOCOLS (Manson, ed.), Pages 1-5 (Humana Press 1992); Coligan et al., Production of Polyclonal Antisera in Rabbits, Rats, Mice and Hamsters, in CURRENT PROTOCOLS IN IMMUNOLOGY, section 2.4.1 (1992), which are incorporated herein by reference. The preparation of monoclonal antibodies is also conventional. See, for example, Kohier & Milstein, Nature 256: 495 (1975); Coligan et al., Sections 2.5.1-2.6.7; and Harlow et al., ANTIBODIES: A LABORATORY MANUAL, page 726 (Cold Spring Harbor Pub. 1988), which are incorporated herein by reference. Briefly, monoclonal antibodies can be obtained by injecting mice with a composition comprising an antigen, verifying the presence of antibody production by analyzing a serum sample., removing the spleen to obtain B lymphocytes, fusing the B lymphocytes with myeloma cells to produce hybridomas, cloning the hybridomas, selecting the positive clones that produce antibodies to the antigen, and isolating the antibodies from the hybridoma cultures. Monoclonal antibodies can be isolated and purified from hybridoma cultures by a variety of well-established techniques. These isolation techniques include affinity chromatography with protein-A sepharose, size exclusion chromatography, and ion exchange chromatography. See, for example, Coligan et al., Sections 2.7.1-2.7.12 and sections 2.9.1-2.9.3; Barnes et al., Purification of Immunoglobulin G (IgG), in METHODS IN MOLECULAR BIOLOGY, VOL. 10, pages 79-104 (Humana Press 1992). The methods of in vitro and in vivo multiplication of monoclonal antibodies are well known to those skilled in the art. In vitro multiplication can be carried out in convenient culture media such as Dulbecco's Modified Eagle Medium of RPMI 1640 medium, optionally filled with a mammalian serum such as fetal calf serum or trace elements and growth-supporting supplements such as such as normal mouse peritoneal exudate cells, spleen cells, bone marrow macrophages. In vitro production provides relatively pure antibody preparations and allows scaling to produce large quantities of the desired antibodies. The large-scale hybridoma culture can be carried out by homogeneous suspension culture in an air-lift reactor, in a continuous agitation reactor, or in an immobilized or entrapped cell culture. Live multiplication can be carried out by injecting mammalian cell clones histocompatible with the parent cells, eg, osingigenic mice, to cause the growth of tumors that produce antibodies. Optionally, the animals are started with hydrocarbon, especially oils such as pristane (tetramethylpentadecane) before injection. After one to three weeks, the desired monoclonal antibody is recovered from the body fluid of the animal. Therapeutic applications of the antibodies described herein are also part of the present invention. With increasing evidence that steroids affect the cell surface and alter ion permeability, as well as the release of neurohormones and neurotransmitters, antibodies to extracellular receptors such as Binl may have therapeutic applications. The antibodies of the present invention can also be derived from subhuman primate antibodies. General techniques for culturing therapeutically useful antibodies in baboons can be found, for example, in Goldenberg et al., International publication WO 91/11465 (1991) and Losman et al. Int. J. Cancer 46: 310 (1990), which are incorporated herein by reference. Alternatively, a therapeutically useful anti-Binl antibody can be derived from a "humanized" monoclonal antibody. Humanized monoclonal antibodies are produced by transferring regions of mouse complementarity determination from heavy and light variable chains of mouse immunoglobulin to a human variable domain, and then substitute human residues in the framework regions of the murine counterparts. The use of antibody components derived from humanized monoclonal antibodies makes obvious the potential problems associated with the immunogenicity of the murine constant regions. General techniques for cloning murine immunoglobulin variable domains are described, for example, by Orlandi et al., Proc. Na t '1 Acad. Sci. USA 86: 3833 (1989), which is hereby incorporated by reference in its entirety. Techniques for producing humanized monoclonal antibodies are described, for example, by Jones et al., Na ture 321: 522 (1986); Riechmann et al., Na ture 332: 323 (1988); Verhoeyen et al., Science 239: 1534 (1988); Carter and collaborators, Proc. Nat 'l Acad. Sci. USA 89: 4285 (1992); Sandhu, Crit. Rev. Biotech. 12: 437 (1992); and Singer et al., J. Immunol. 159: 2844 (1993), which are incorporated herein by reference. The antibodies of the invention can also be derived from human antibody fragments isolated from a combinatorial immunoglobulin library. See, for example, Barbas et al., METHODS: A COMPANION TO METHODS IN ENZYMOLOGY, VOL. 2, page 119 (1991); Winter et al., Aan Rev. Immunol. 12: 433 (1994), which are incorporated herein by reference. Expression and cloning vectors that are useful for producing a human immunoglobulin phage library can be obtained, for example, from STRATAGENE Cloning Systems (La Jolla, CA). In addition, the antibodies of the present invention can be derived from a human monoclonal antibody. These antibodies are obtained from transgenic mice that have been "engineered" to produce specific human antibodies in response to antigenic stimulation. In this technique, elements of human heavy and light chain sites are introduced into strains of mice derived from embryonic stem cell lines containing target breaks of the endogenous heavy and light chain sites. Transgenic mice can synthesize human antibodies specific for human antigens and can be used to produce hybridomas that secrete human antibodies. Methods for obtaining human antibodies from transgenic mice are described by Green et al., Na ture Genet. 7:13 (1994); Lonberg et al., Na ture 368: 856 (1994); and Taylor et al., In t. Immunol. 6: 579 (1994), which are incorporated herein by reference. The antibody fragments of the present invention can be prepared by proteolytic hydrolysis of the antibody or by expression in E. Nucleic acid coli encoding the fragment. Antibody fragments can be obtained by digestion of pepsin or papain from whole antibodies by conventional methods. For example, fragments of antibodies can be produced by enzymatic cleavage of antibodies with pepsin to provide a 5S fragment denoted F (ab ') 2. This fragment can be further dissociated using a thiol reducing agent, and optionally a blocking group for the sulfhydryl groups resulting from disulfide disulfide linkages, to produce 3.5S Fab 'monovalent fragments. Alternatively, an enzymatic dissociation using pepsin produces two monovalent Fab 'fragments and one Fc fragment directly. These methods are described, for example, by Goldenberg, U.S. Patent Nos. 4,036,945 and U.S. 4,331,647, and the references contained therein. These patents are hereby incorporated by reference in their entirety. See also Nisonhoff et al., Arch. Biochem. Biophys. 89: 230 (1960); Porter, Biochem. J. 73: 119 (1959); Edelman et al., METHODS IN ENZYMOLOGY, VOL. 1, page 422 (Academic Press 1967); and Coligan et al., in sections 2.8.1-2.8.10 and 2.10.1-2.10.4. Other methods of dissociating antibodies, such as removal of heavy chains to form monovalent light-heavy chain fragments, further fragment dissociation, or other enzymatic, chemical or genetic techniques can also be used, as the fragments are linked to the antigen that is recognized by the intact antibody. For example, the Fv fragments comprise an association of VH and VL chains. This association may be non-covalent, as described in Inbar et al., Proc. Nat '1 Acad. Sci. USA 69: 2659 (1972). Alternatively, the variable chains can be linked through an intermolecular or crosslinked disulfide bond by chemicals such as glutaraldehyde. See, for example, Sandhu, previously in this. Preferably, the Fv fragments comprise VH and VL chains connected by a peptide linker. These single chain antigen binding proteins (sFv) are prepared by constructing a structural gene comprising nucleic acid sequences encoding the VH and VL domains connected by an oligonucleotide. The structural gene is inserted into an expression vector, which is subsequently introduced into a host cell such as E. coli. Recombinant host cells synthesize a single polypeptide chain with a linker peptide that bypasses the two V domains. Methods for producing sFvs are described, for example, by Whitlow et al., METHODS: A COMPANION TO METHODS IN ENZYMOLOGY, VOL. 2, page 97 (1991); Bird et al., Science 242: 423-426 (1988); Ladner et al., U.S. Patent No. 4,946,778; Pack et al., Bio / Technology 11: 1271-77 (1993); and Sandhu, upra. Another form of the antibody fragment is a peptide encoding a single region of complementarity determination (CDR). CDR peptides ("minimum recognition units") can be obtained by constructing genes encoding the CDR of an antibody of interest. These genes are prepared, for example, using the polymerase chain reaction to synthesize the variable region of the RNA of the cells that produce antibodies. See, for example, Larrick et al., METHODS: A COMPANION TO METHODS IN ENZYMOLOGY, VOL. 2, page 106 (1991). The term "antibody" as used in this invention includes intact molecules as well as fragments thereof, such as Fab, F (ab ') 2. and Fv which are capable of binding to an epitope determinant present in the Binl polypeptide. These antibody fragments retain some ability to selectively bind with their antigen or receptor. As used in this invention, the term "epitope" refers to an antigenic determinant or an antigen to which the paratope of an antibody binds. Epitope determinants usually consist of chemically active surface groupings of molecules such as amino acids or sugar side chains and usually have specific three-dimensional structural characteristics, as well as specific charge characteristics. Antibodies that bind to the Binl polypeptide of the invention can be prepared using an intact polypeptide or fragments containing small peptides of interest as the immunizing antigen. For example, it may be desirable to produce antibodies that specifically bind to the N or C terminal domains of Binl. The polypeptide or peptide used to immunize an animal that is derived from translated or chemically synthesized cDNA that can be conjugated to a carrier protein, if desired. These commonly used carriers which are chemically coupled to the immunizing peptide include keyhole limpet hemocyanin (KLH), thyroglobulin, bovine serum albumin (BSA), and tetanus toxoid. The polyclonal or monoclonal antibodies of the invention can be further purified, for example, by attaching them to and separating them from a matrix to which the polypeptide or peptide to which the antibodies are generated is attached. Those skilled in the art will know several techniques common in immunological techniques for purification and / or concentration of polyclonal antibodies, as well as monoclonal antibodies (see for example, Coligan et al., Unit 9, Current Protocols in Immunology, Wiley Interscience, 1994, incorporated. by reference). It is also possible to use the anti-idiotype technology to produce monoclonal antibodies of the invention which mimic an epitope. For example, the anti-idiotypic monoclonal antibody made to a first monoclonal antibody will have a binding domain in the hypervariable region which is the "image" of the epitope bound by the first monoclonal antibody. GENETICALLY MODIFIED VEGETABLES AND METHODS OF MAKING THEM In another embodiment, the invention provides a method for producing a genetically modified plant characterized by having an increased yield as compared to a plant that has not been genetically modified (e.g., a wild-type plant). The term "yield" has been previously defined herein. The method of the invention comprises the steps of introducing at least one nucleic acid sequence encoding Binl, into a plant cell to obtain a transformed plant cell wherein the nucleic acid sequence is operably associated with a promoter, producing a plant from the transformed plant cell under conditions that allow expression of the Binl polypeptide; and after that select a vegetable that exhibits increased yield. The term "genetic modification" as used herein refers to the introduction of one or more heterologous nucleic acid sequences in one or more plant cells, to provide viable, sexually competent vegetables. The term "genetically modified" as used herein refers to a plant that has been generated through the aforementioned process. The genetically modified plants of the invention are capable of self-pollination or cross-pollination with other plants of the same species so that the foreign gene, carried in the germ line, can be inserted into or cultivated in agriculturally useful plant varieties. The term "plant cell" as used herein refers to protoplasts, cells that produce gametes, and cells that regenerate into whole plants. In accordance with the above, a seed comprising multiple plant cells capable of regeneration in a whole plant is included in the definition of "plant cell". As used herein, the term "plant" refers to either an entire vegetable, a vegetable part, a plant cell, or a group of plant cells, such as plant tissue, for example. Plants are also included within the meaning of "vegetable". The plants included in the invention are any vegetable amenable to transformation techniques, including angiosperms, gymnosperms, monocotyledons and dicotyledons. Examples of monocotyledon plants include, but are not limited to, asparagus, field and sweet corn, barley, wheat, rice, sorghum, onion, pearl millet, rye and oats. Examples of dicotyledon plants include, but are not limited to tomato, tobacco, cotton, rapeseed, beans, soybeans, potatoes, grapes, strawberries, chilies, lettuce, peas, alfalfa, cloves, cabbage crops or Brassica olerácea ( for example, cabbage, broccoli, cauliflower, Brussels sprouts), radish, carrot, betavel, eggplant, spinach, cucumber, squash, watermelon, melon, sunflower and several ornamentals. Wood species include poplar, pine, redwood, cedar, oak, and so on. The term "heterologous nucleic acid sequence" as used herein refers to a nucleic acid foreign to the receiving host plant, or native to the host if the native nucleic acid is substantially modified from its original form. For example, the term includes a nucleic acid originating in the host species, wherein this sequence is operably linked to a promoter that differs from the native or original type promoter. In the broad method of the invention, at least one nucleic acid sequence encoding the Bin1 polypeptide is associated with a convenient promoter. It may be desirable to introduce more than one copy of Binl polynucleotide into a plant for increased Binl expression. For example, multiple copies of the gene would have the effect of increasing the production of Binl polypeptide in the plant by allowing a greater brassinosteroid action or other steroid / hormone action. The genetically modified plants of the present invention are produced by introducing into a plant cell, a vector that includes at least one nucleic acid sequence encoding Binl. To be effective once introduced into the plant cell, the Binl nucleic acid sequence must be operably associated with a promoter that is effective in plant cells to cause Binl transcription. Additionally, a polyadenylation or transcription control sequence, also recognized in plant cells, may also be employed. It is preferred that the vector carrying the nucleic acid sequence to be inserted also contains one or more selectable marker genes so that the transformed cells can be selected from untransformed cells in culture, as described herein. The term "operably associated" refers to a functional link between a promoter sequence and the Binl nucleic acid sequence regulated by the promoter. The linked promoter operably controls the expression of the Binl nucleic acid sequence. The expression of Binl polynucleotides in the present invention can be driven by several promoters. Although the endogenous promoter, or natural of a structural gene of interest can be used for transcription regulation of the gene, preferably, the promoter is a foreign regulatory sequence. For plant expression vectors, suitable viral promoters include the 35S RNA and 19S RNA promoters of CaMV (Brisson et al., Na ture, 310: 511, 1984; Odell et al., Na ture, 313: 810, 1985); the full-length transcription promoter of fig mosaic virus (FMV) (Gowda et al., J. Cell Biochem., 13D: 301, 1989) and the coating protein promoter for TMV (Takamatsu et al., EMBO J. .6: 307, 1987). Alternatively, plant promoters such as the light-inducible promoter from the subunit or small unit of ribulose bisphosphate carboxylase (ssRUBISCO) (Coruzzi et al., EMBO J., 3: 1671, 1984; Broglie et al., Science, 224 : 838, 1984); the mannopin synthase promoter (Velten et al., EMBO J., 73: 2723, 1984) the nopaline synthase (NOS) and octopine synthase (OCS) promoters (carried in plasmids that induce Agrobacterium tumefaciens tumors) or heat shock promoters, for example, soybean hsp 17.5-E or hsp 17.3-B (Gurley et al., Mol Cell Biol. 6: 559, 1986; Severin et al., Plant Mol. Biol. 5: 827, 1990) can be used. . Promoters useful in the invention include both the constitutive and inducible natural promoters as well as the manipulated promoters. The CaMV promoters are examples of constitutive promoters. To be more useful, an inducible promoter should 1) provide low expression in the absence of the inducer; 2) provide high expression in the presence of the inducer; 3) use an induction scheme that does not interfere with the normal physiology of the plant; and 4) have no effect on the expression of other genes. Examples of inducible promoters useful in plants include those induced by chemical means, such as the promoter of yeast metallothionein that is activated by copper ions (Mett et al., Proc. Nati. Acad. Sci. U. S. A.,. 90: 4567, 1993); regulatory sequences In2-1 and In2-2 which are activated by substituted benzenesulfonamides, for example, herbicidal insurers (Hershey et al., Plant Mol. Biol., /17.:679, 1991); and GRE regulatory sequences that are induced by glucocorticoids (Schena et al., Proc.Nat.Acid.Sci., U.S.A. 88.:10421, 1991). Other promoters, both constitutive and inducible, will be known to those skilled in the art. The particular promoter selected should be capable of causing sufficient expression to result in the production of an effective amount of structural gene product, for example, Binl polypeptide to cause increased plant biomass, and thus increased yield. The promoters used in the vector constructions of the present invention can be modified, if desired, to affect their control characteristics. Tissue-specific promoters can also be used in the present invention. As an example of a tissue-specific promoter is the active promoter in shoot meristems (Atanassova et al., Plant J., 2.:291, 1992). Other tissue-specific promoters useful in transgenic plants, including the cdc2a promoter and the cyc07 promoter, will be known to those skilled in the art. (See, for example, Ito et al., Plant Mol. Biol., 24: 863, 1994, Martinez et al., Proc. Na ti, Acad. Sci. USA, .89: 7360, 1992, Medford et al., Plant Cell. , 3: 359, 1991; Terada, et al., Plant Journal, 3: 241, 1993; Wissenbach et al., Plant Journal, 4: 411, 1993). There are known promoters that limit expression to particular plant parts or in response to particular stimuli. For example, potato-specific promoters of potato, such as patatin promoters or promoters of large or small subunits of ADP glucose pyrophosphorylase, could be operatively associated with Binl to provide expression primarily in the tuber and thus provide resistance to attacks on the tuber, such as by Erwinia. A specific fruit promoter would be desirable to impart resistance to Botrytis in strawberries or grapes. A specific root promoter would be desirable to obtain the expression of Binl roots of wheat or barley to provide resistance to Ggt. One skilled in the art will know many of these plant part specific promoters that would be useful in the present invention. Alternatively, the promoters used can be selected to confer specific expression of Binl in response to fungal infection. Infection of plants by fungal pathogens activates genes related to defense or related to pathogenesis (PR) that encode (1) enzymes involved in the metabolism of phenylpropanoid such as - the lyase phenylalanine ammonia, chalcone synthase, 4-coumarate coA ligase and coumaric acid 4-hydroxylase, (2) proteins that modify plant cell walls such as glycoproteins rich in hydroxyproline, glycine-rich proteins, and peroxidases, (3) enzymes, such as chitinases and glucanases, that degrade the cell wall of the fungus , (4) proteins similar to thaumatin, or (5) proteins of function not yet known. The genes related to defense or related to pathogenesis have been isolated and characterized from several plant species. Promoters of these genes can be used to obtain expression of Binl in transgenic plants when these plants are stimulated with a pathogen, particularly a fungal pathogen such as Pi. The particular promoter selected should be capable of causing sufficient expression of Binl to result in the production of an effective amount of polypeptide. The promoters used in the nucleic acid constructs of the present invention can be modified, if desired, to affect their control characteristics. For example, the CaMV 35S promoter can be ligated to the portion of the ssRUBISCO gene that represses the expression of ssRUBISCO in the absence of light, to create a promoter that is active in the leaves but not in the roots. The resulting chimeric promoter can be used as described herein. For the purposes of this description, the phrase "CaMV 35S" promoter thus includes variations of the CaMV 35S promoter, for example promoters derived by means of binding to operator regions, random or controlled mutagenesis, and so on. In addition, promoters can be altered to contain multiple "enhancer sequences" to help elevate gene expression. Optionally, a selectable marker can be associated with the nucleic acid sequence to be inserted.

As used herein, the term "marker" refers to a gene that encodes a trait or phenotype which allows the selection of, or classification of, a plant or plant cell that contains the marker. Preferably, the marker gene is an antibiotic-resistant gene by which the appropriate antibiotic can be used to select transformed cells between cells that are not transformed. Examples of suitable selectable markers include adenosine deaminase, dihydrofolate reductase, hygromycin-B-phosphotransferase, thymidine kinase, xanthine-guanine phospho-ribosyltransferase and aminoglycoside 3 '-O-phosphotransferase II (resistance to kanamycin, neomycin and G418). Other convenient markers will be known to those skilled in the art. The vectors employed in the present invention for the transformation of plant cells comprise a sequence of nucleic acids encoding the Bin1 polypeptide, operably associated with a promoter. In order to effect a transformation process according to the present invention, it is first necessary to construct a suitable vector and introduce it appropriately into the plant cell. The details of the. construction of the vectors used herein are known to those skilled in the art of plant genetic engineering. The Binl nucleic acid sequences used in the present invention can be introduced into plant cells using Ti plasmids from Agrobacterium tumefaciens, root-inducing plasmids (Ri), and plant virus vectors. (For reviews of these techniques see, for example, Weissbach &Weissbach, 1988, Methods for Plant Molecular Biology, Academic Press, NY, Section VIII, pp. 421-463; and Grierson &Corey, 1988, Plant Molecular Biology, 2d Ed., Blackie, London, Ch. 7-9, and Horsch, et al., Science, 227: 1229, 1985, both incorporated herein by reference). In addition to the plant transformation vectors derived from the Ti plasmids or the root inducer (Ri) of agrobacterium, alternative methods of transformation can be used, including the use of liposomes, electroporation, chemicals that increase the absorption of free nucleic acid, transformation using virus or pollen and the use of biolistic transformation. One skilled in the art will be able to select a suitable vector for introducing the Binl polynucleotide sequence into a relatively intact state. Thus, any vector which will produce a plant carrying the introduced nucleic acid sequence should be sufficient. Even the use of a naked piece of nucleic acid would be expected to confer the properties of this invention, albeit at low efficiency. The selection of the vector, or if using a vector, is typically guided by the selected transformation method. The transformation of vegetables according to the invention can be carried out essentially in any of the ways known to those skilled in the art of plant molecular biology. (See, for example, Methods of Enzymology, Vol. 153, 1987, Wu and Grossman, Eds., Academic Press, incorporated herein by reference.) As used herein, the term "transformation" means alteration of the genotype of a host plant by the introduction of the Binl nucleic acid sequence. For example, the Binl nucleic acid sequence can be introduced into a plant cell using Agroba cterium tumefa ciens containing the Ti plasmid, as briefly mentioned above. When using a culture of A. As a vehicle for transformation, it is advantageous to use a non-oncogenic strain of Agrobacterium as the vector carrier so that normal non-oncogenic differentiation of the transformed tissues is possible. It is also preferred that the agrobacteria host a binary Ti plasmid system. This binary system comprises 1) a first Ti plasmid that has a virulence region essential for the introduction of transfer nucleic acid (T-DNA) in plants, and 2) a chimeric plasmid. The latter contains at least one border region of the T-DNA region of a wild-type Ti plasmid flanking the nucleic acid to be transferred. It has been shown that binary Ti plasmid systems are effective in transforming plant cells (De Framond, Biotechnology, .1: 262, 1983; Hoekema et al., Na ture, 303: 179, 1983). This binary system is preferred because it does not require integration into the Ti plasmid of agrobacterium, which is an older methodology. Methods involving the use of agrobacterium for transformation according to the present invention include, but are not limited to: 1) Agrobacterium cocultivation with cultured isolated protoplasts; 2) transformation of plant cells or tissues with Agrobacterium; or 3) transformation of seeds, apices or meristems with Agrobacterium. In addition, gene transfer can be carried out by in-plant transformation by Agrobacterium, as described by Bechtold et al., (C. R. Acad. Sci. Paris, 316: 1194, 1993) and exemplified in the examples herein. . This approach is based on vacuum infiltration or immersion of a suspension of Agrobacterium cells. The preferred method for introducing the Binl polynucleotide into plant cells is to infect these plant cells, such as explant, a meristem or a seed, with transformed Agrobacterium tumefaciens as described above. Under suitable conditions known in the art, the transformed plant cells are grown to form suckers, roots, and then grown as plants. Alternatively, the Binl polynucleotide can be introduced into a plant cell using mechanical or chemical elements. For example, the nucleic acid can be mechanically transferred to the plant cell by microinjection using a micropipette. Alternatively, the nucleic acid can be transferred to the plant cell using polyethylene glycol which forms a precipitation complex with genetic material that is picked up by the cell. The Binl polynucleotide can also be introduced into plant cells by electroporation (Fromm, et al, Proc.Na.I. Acad. Sci., U. S.A., 82.:5824, 1985, which is incorporated herein by reference). In this technique, plant protoplasts are electroporated in the presence of vectors or nucleic acids containing the relevant nucleic acid sequences. The electrical impulses of high field strength reversibly permeabilize the membranes allowing the introduction of nucleic acids. Protoplasts of electroporated vegetables reform the cell wall, divide and form a vegetable callus. The selection of transformed plant cells with the transformed gene can be carried out using phenotypic labels as described herein. Another method to introduce the Binl polynucleotide into a plant cell is the high speed ballistic penetration by small particles with the nucleic acid to be introduced content either within the matrix of these particles, or on the surface thereof (Klein). et al., Na ture 327: 70, 1987). Bombardment transformation methods are also described in Sanford, et al.,. { Techniques 3: 3-16, 1991) and Klein et al.,. { Bio / Techniques 10 .: 286, 1992). Although typically only a single introduction of new nucleic acid sequence is required, this method particularly provides multiple introductions. Cauliflower mosaic virus (CaMV) can also be used as a vector for introducing nucleic acid into plant cells (U.S. Patent No. 4,407,956). The CaMV viral nucleic acid genome is inserted into the parent bacterial plasmid creating a recombinant nucleic acid molecule that can be propagated as a bacterium. After cloning, the recombinant plasmid can again be cloned and further modified by introducing the desired nucleic acid sequence. The modified viral portion of the recombinant plasmid is separated from the parent bacterial plasmid, and used to inoculate plant cells or plants. As used herein, the term "making contact" refers to any means of introducing Binl into the plant cell, including the chemical and physical means as described above. Preferably, contacting refers to introducing the nucleic acid or vector into plant cells (including an explant, a meristem or a seed), via Agrobacterium tumefaciens transformed with nucleic acid encoding Binl as described above. Normally, a transformed plant cell is regenerated to obtain an entire plant from the transformation process. The immediate product of the transformation is called "transgenote". The term "growth" or "regeneration" as used herein means growing an entire plant from a plant cell, a group of plant cells, a plant part (including the seeds), or a piece of plant (for example example, from a protoplast, callus or part of a tissue). The regeneration of protoplasts varies from one species to another, but generally the process starts first by providing a protoplast suspension. In certain species, the formation of plants can be induced from the suspension of protoplasts, followed by putrefaction and germination as a natural plant. The culture medium usually contains several amino acids and hormones, necessary for growth and regeneration. Examples of hormones used include auxins and cytokinins. It is sometimes advantageous to add glutamic acid and proline to the medium, especially for plant species such as corn and alfalfa. Efficient regeneration will depend on the medium, the genotype, and the history of the crop. If these variables are controlled, the regeneration is reproducible. Regeneration also occurs from plant calluses, explant, organs or plant parts. The transformation can be performed in the context of organ or plant part regeneration (see Methods in Enzymology, Vol. 118 and Klee, et al., Annual Review of Plant Physiology, 38: 467, 1987). When using the leaf disc transformation regeneration method of Horsch, et al., Science, 227: 1229, 1985, the discs are grown on selective medium, followed by formation of shoots in approximately 2-4 weeks. The shoots that develop are separated from the calluses and transplanted into suitable selective media that induce root. Root shoots are transplanted to the ground as soon as possible after the roots appear. The shoots can be replanted as required, until they reach maturity. In vegetatively propagated crops, mature transgenic plants are propagated using cut techniques or tissue culture techniques to produce multiple identical plants. The selection of desirable transgenotes is made and new varieties are obtained and propagated vegetatively for commercial use. In propagated seed crops, mature transgenic plants self-cross to produce a homozygous inbred plant. The resulting inbred plant produces seeds that contain the recently introduced foreign gene. These seeds can be grown to produce plants that would produce the selected phenotype eg increased yield. The parts obtained from the regenerated plant, such as flowers, seeds, leaves, branches, roots, fruits, and the like, are included in the invention, provided that these parts comprise cells that have been transformed as described. Progeny and variants, and mutants of the regenerated plants will also be included within the scope of the invention, provided that these parts comprise the introduced amino acid sequences. Plants that exhibit increased yield or biomass compared to wild-type plants can be selected by visual observation. The invention includes plants produced by the method of the invention, as well as plant tissue and seeds. In still another embodiment, the invention provides a method for producing a genetically modified plant characterized by having increased yield as compared to the plant of the wild type. The method includes introducing at least one nucleic acid sequence encoding the Binl polypeptide into a plant cell to obtain a transformed plant cell.; culturing the transformed plant cell under conditions that allow expression of the Binl polypeptide to obtain a plant that has increased yield. Conditions such as the environment and conditions that induce the promoter may vary from one species to another, but they should be the same within a species. In another embodiment, the invention provides a method for producing a plant characterized by having increased yield by contacting a susceptible plant with an amount of Binl promoter inducer of an agent that induces the expression of the Binl gene, wherein the induction of expression of the Binl gene results in the production of a plant that has increased yield compared to a plant that does not make contact with the agent. A "susceptible vegetable" refers to a plant that can be induced to use its endogenous Binl gene to achieve increased yield. The term "promoter-inducing amount" refers to the amount of agent necessary to elevate the expression of the Binl gene on the expression of Binl in a plant not contacted with the agent. For example, a transcription factor or a chemical agent can be used to elevate gene expression from the native Binl promoter. Alternatively, the Binl promoter can be a heterologous promoter capable of induction. The method of the invention considers contacting cells containing endogenous Binl promoter or recombinantly produced Binl promoter. PATHOGEN RESISTANT PLANTS In another aspect of the invention, it is considered that the increased expression of Binl in a plant cell or in a plant increases the resistance of the cell / plant to plant pests or plant pathogens. For example, field studies have shown that brasinolides are effective as pesticides, therefore, increased expression of Binl would result in increased amounts of brasino-roides receptor in the plant. In addition, increased expression of Binl can also cause increased resistance to pesticides (insurers). The Binl therefore protects plants against pests as well as against pesticides. In still another embodiment, the invention provides a method for producing genetically transformed plants, resistant to disease, comprising introducing into the genome of a plant cell to obtain a transformed plant cell, a nucleic acid construct comprising (i) a promoter which works in plant cells to cause the production of an RNA sequence; and (ii) a nucleic acid sequence encoding the Bin1 polypeptide; and regenerating from the transformed plant cell genetically transformed plants which express the Binl polypeptide in an amount effective to inhibit infection by bacterial pathogens or fungi. The invention includes plants, seeds, et cetera, produced by the method of the invention. As used herein, the term "pathogen resistance" is used to indicate that it causes a reduction in damage to a plant or crop due to infection by a bacterial pathogen or fungus. The method of the invention is useful for inhibiting the growth of pathogens of agriculturally important fungi, including, Verticill ium dahl iae, one of the most widespread and harmful plant pathogens, which causes disease in many plants, Phytoph thora infestans (Pi), the pathogen responsible for late rust disease in potatoes and tomatoes, Botrytis cinerea (Be), the origin of gray mold in various fruits and vegetables, Septoria nodorum (Sn), the causal agent of yellow spot in wheat, Pseudocercosporella herpotrichoides ( Ph), the causative agent of detrigid skin stain and Gaeumannomyces graminis var tritici (Ggt), the causative agent of the disease attacks all in cereals and Erwinia carotovora, the causal agent of soft potato rot, a disease after harvest of the potatoes. TRANSGENIC ANIMALS In another modality, the present invention relates to transgenic animals that have cells expressing a homolog of the plant Binl. While not wishing to be bound by a particular theory, it is believed that a mammalian homologue of the Binl polypeptide of the invention would bind to mammalian steroids. Other homologs of the Binl polypeptide and polynucleotide of the invention are also included herein. These transgenic animals represent a model system for the study of steroid-receptor interaction and link to develop more effective therapies. The term "animal" denotes here a mammalian species except human. It also includes an individual animal at all stages of development, including embryonic and fetal stages. Farm animals (pigs, goats, sheep, cows, horses, rabbits and the like), rodents (such as mice), and domestic animals (e.g., cats and dogs) are included within the scope of the present invention. A "transgenic" animal is any animal that contains cells that carry genetic information received, directly or indirectly, by deliberate genetic manipulation at the subcellular level, such as by microinjection or infection with recombinant virus. "Transgenic" in the present context does not cover classical crosses or in vitro fertilization, but denotes animals in which one or more cells receive a recombinant nucleic acid molecule. Although it is highly preferred that this molecule be integrated into the chromosomes of the animal, the present invention also contemplates the use of extrachrome-somal replication nucleic acid sequences, such as could be overlapped in yeast artificial chromosomes. The term "transgenic animal" also includes a transgenic animal of "germ cell line". A transgenic animal of germ cell line is a transgenic animal in which the genetic information has been collected and incorporated into a germ line cell, thus obtaining the capacity to transfer the information to the descendants. If these descendants do in fact possess some or all of that information, then they, too, are transgenic animals. The term "transgenic" as used herein additionally includes any organism whose genome has been altered by in vitro manipulation of the initial embryo or fertilized egg or by any transgenic technology to induce an elimination of a specific gene. The term "gene elimination" as used herein, refers to the targeted disruption of a gene in vivo with the complete loss of function that has been achieved by any transgenic technology familiar to those skilled in the art. In one embodiment, transgenic animals that have gene deletions are those in which the target gene has become non-functional through an insertion directed to the gene that is to become non-functional by homologous recombination. As used herein, the term "transgenic" includes any transgenic technology familiar to those skilled in the art that can produce an organism carrying an introduced transgene or one in which an endogenous gene has become non-functional or eliminated. The transgene to be used to practice the present invention is a nucleic acid sequence encoding Binl or a nucleic acid sequence comprising a modified Binl coding sequence. In one embodiment, the nucleic acid encoding Binl is the transgene, resulting in cells expressing Binl. The Binl can be either the wild-type, original sequence, such as a homolog presented in SEQ ID NO: 1, or a modified sequence, such as a mutant having a G611Q alteration.

In another embodiment, the mammalian Binl homologous gene is disrupted by attacking the homolog in embryonic stem cells. For example, the entire mature N-terminal region of the Binl gene can be suppressed, resulting in the expression of a truncated receptor. Optionally, the interruption or deletion of Binl may be accompanied by insertion or replacement with another nucleic acid sequence, such as a non-functional Binl sequence. In yet other embodiments, the transgene comprises anti-sense nucleic acid for the coding sequence for Binl. In another embodiment, the transgene comprises nucleic acid encoding an antibody or receptor peptide sequence that is capable of binding to Binl. Where appropriate, nucleic acid sequences encoding proteins that have Binl activity but differ in nucleic acid sequences due to the degeneracy of the genetic code, as well as truncated forms, allelic variants and interspecies homologs may also be used herein. . B ± nl VARIANTS The term "Binl variant" as used herein means a molecule that simulates at least part of the structure of Binl and binds brassinosteroids. Binl variant homologs may also be useful to prevent steroid binding, thus preventing maturation of the oocyte, for example, or maintaining a plant in a vegetative state, as compared to the senescent state.

In one embodiment, the present invention relates to peptides and peptide derivatives that have fewer amino acid residues than Binl and retain the ability to bind brassinosteroids. These peptides and peptide derivatives could represent useful research and diagnostic tools in the study of steroids that come together and the development of more effective therapies and contraceptives. The Binl fragments according to the invention include those corresponding to the Binl regions that are proposed to bind to the brassinosteroids, for example, amino acid residues 588 to 649 of SEQ ID NO: 2, which are disclosed in the cell surface. Binl can be altered by changing the nucleic acid that encodes the protein. Preferably, only conservative amino acid alterations are considered, using amino acids having the same or similar properties. Illustrative amino acid substitutions include changes of alanine by serine; arginine for lysine; asparagine by glutamine or histidine; aspartate for glutamate; cysteine by serine; glutamine by asparagine; glutamate by aspartate; glycine by proline; histidine by asparagine or glutamine; isoleucine by leucine or valine; leucine by valine or isoleucine; lysine by arginine, glutamine, or glutamate; methionine by leucine or isoleucine; phenylalanine by tyrosine, leucine or methionine; serine by threonine; threonine by serine; tryptophan by tyrosine; tyrosine by tryptophan or phenylalanine; valine by isoleucine or leucine. The variants useful for the present invention comprise Binl analogs, homologs, muteins and mimetics that retain protein kinase activity. Binl peptides refer to portions of the amino acid sequence of Binl that also retain this capacity. The variants can be generated directly from Binl itself by chemical modification, by digestion of proteolytic enzyme, or by combinations thereof. Additionally, genetic engineering techniques, as well as methods for synthesizing polypeptide directly from amino acid residues, can be employed. The peptides of the invention can be produced by standard recombinant methods or synthesized by these commonly used methods such as t-BOC or FMOC protection of alpha-amino groups. Both of these latter methods involve stepped synthesis whereby a single amino acid is added at each step beginning with the C-terminus of the peptide (see, Coligan, et al., Current Protocols in Immunology, Wiley Interscience, 1991, Unit 9). The peptides of the invention can also be synthesized by well-known solid phase peptide synthesis methods described by (Merrifield, J. Ambiente Chem. Soc., 85 .: 2149, 1962), and Stewart and Young, Solid Phase Peptides Synthesis. , (Freeman, San Francisco, 1969, pp. 27-62), using a copoly (styrene-divinylbenzene) containing 0.1-1.0 mMol amines / per gram of polymer. Upon completion of the chemical synthesis, the peptides can be deprotected and dissociated from the polymer by treatment with liquid HF-10% anisole for about 1 / 4-1 hours at 0 ° C. After the evaporation of the reagents, the peptides are extracted from the polymer with a 1% acetic acid solution which is lyophilized to produce the crude material. This can usually be purified by techniques such as gel filtration on Sephadex G-15 using 5% acetic acid as a solvent. The lyophilization of suitable fractions from the column will give the homogeneous peptide or the peptide derivatives, which can then be characterized by standard techniques such as amino acid analysis, thin layer chromatography, high performance liquid chromatography, ultraviolet absorption spectroscopy, rotation molar, solubility, and quantify by Edman degradation in solid phase. The term "substantially purified" as used herein refers to a molecule, such as a peptide that is substantially free of other proteins, lipids, carbohydrates, nucleic acids, and other biological materials with which it naturally associates. For example, a substantially pure molecule, such as a polypeptide, can be at least 60%, by dry weight, the molecule of interest. One skilled in the art can purify Binl peptides using standard protein purification methods and the purity of the polypeptides can be determined using standard methods including, for example, polyacrylamide gel electrophoresis (e.g., SDS-PAGE), column chromatography (e.g., high performance liquid chromatography (HPLC)), and amino terminal amino acid sequence analysis. Compounds that are not peptides that mimic the binding and function of Binl ("mimetics") can be produced by the approach outlined in Saragovi et al., Science 253: 792-95 (1991). Mimetics are molecules that mimic elements of secondary protein structure. See, for example, Johnson et al., "Peptide Turn My etics", in BIOTECHNOLOGY AND PHARMACY, Pezzuto et al., Eds., (Chapman and Hall, New York 1993). The underlying reasoning behind the use of peptide mimetics is that the central structure of the peptide in proteins exists mainly to orient the side chains of amino acids in a way that facilitates molecular interactions. For the purposes of the present invention, suitable mimetics can be considered as equivalent to Binl itself. Longer peptides can be produced by "original chemical" ligation techniques that link peptides together (Dawson, et al., Science, 266: 776, 1994). The variants can be created by recombinant techniques employing cDNA or genomic cloning methods. Site-specific mutagenesis techniques directed to the region may also be employed. See CURRENT PROTOCOLS IN MOLECULAR BIOLOGY Vol. 1, ch. 8 (Ausubel et al., Eds., J. Wiley & amp; amp;; Sons 1989 & Supp. 1990-93); PROTEIN ENGINEERING (Oxender &Fox eds., A. Liss, Inc. 1987). In addition, techniques mediated by polymerase chain reaction and scan-linker for mutagenesis can be employed. See PCR TECHNOLOGY (Eriich ed., Stockton Press 1989); CURRENT PROTOCOLS IN MOLECULAR BIOLOGY, vols. 1 & 2, supra. Protein sequencing, structure and modeling approaches for use with any of the above techniques are described in PROTEIN ENGINNERING, loe. cit. , and CURRENT PROTOCOLS IN MOLECULAR BIOLOGY, vols. 1 & 2, upra. BINDING AND BLOCKING AGENTS Binl In still another embodiment, the present invention relates to Binl binding agents that block the binding of brassinosteroids with the Binl receptor polypeptide. In addition, the binding or blocking agents may be useful for Binl receptor homologs in the mammalian system. These agents could represent research and diagnostic tools in the study of steroid binding and cellular responses as well as the development of more effective therapies. Steroids have recently been shown to have effects on neurosecretion and on the entry or mobilization of Ca2 + in the cell (McEwen, B., TIPS, Elsevier Science Publishers Ltd. (UK), 1991, Vol. 12, pp. 141-147). Binl binding or blocking agents are also effective, for example, in maintaining a plant in the vegetative state. Binl receptor deficiency can also be associated with male infertility, therefore, blocking the brassinosteroid that binds to Binl can be a useful contraceptive regimen. In addition, inhibition of Binl can be associated with the inhibition of oocyte maturation. In the context of the brassinosteroid linkage with Binl, the phrase "Binl binding agent" denotes a ligand that naturally occurs from Binl such as, for example, a brassinosteroid or other hormone, a synthetic Binl ligand, or suitable derivatives of the natural or synthetic ligands, as well as small molecules. The determination and isolation of ligands is well described in the art. See, for example, Lerner, Trends Neuro Sci. 17: 142-146 (1994) which is incorporated herein by reference in its entirety. Binl binding agent that blocks the brassinosteroid that binds to Binl is convenient according to the invention to keep the plants in a longer vegetative state, for example. SELECTION FOR LINKING AGENTS AND BINL BLOCKING In another embodiment, the invention provides a method for identifying a binding or blocking agent, which binds to Binl or blocks the steroid binding to the Binl polypeptide. The method includes incubating components comprising the Binl agent and polypeptide under conditions sufficient to allow the components to interact to form a polypeptide / agent complex and detect the presence of the peptide-binding agent by size separation, physical separation, or other standard methods. Agents that bind to Binl include peptides, peptidomimetics, polypeptides, chemical compounds, small molecules and biological agents as described above. In addition to the inhibition of brassinosteroid binding, a person skilled in the art could select the inhibition of Binl that binds to a hormone to determine whether a compound or agent was a binding or blocking agent of the Binl polypeptide. The incubation includes conditions that allow contact between the agent and the Binl polypeptide. The contact includes in solution and in solid phase. The test agent optionally can be a combinatorial library that allows to select a plurality of agents. The agents identified in the method of the invention can be further evaluated, detected, cloned, sequenced and the like, either in solution or after binding to a solid support, by any method usually applied to the detection of a small molecule or a sequence of specific nucleic acid. Nucleic acid sequences can be analyzed by commonly used techniques such as polymerase chain reaction, restriction of oligomer (Saiki, et al., Bio / Technology, 3: 1008-1012, 1985), allele-specific oligonucleotide probe (ASO) analysis (Conner, et al., Proc. Na ti. Acad. Sci. USA, 80: 278, 1983), oligonucleotide ligation assays (OLA) (Landegren, et al., Science, 241: 1011, 1988), and the like. Molecular techniques for nucleic acid analysis have been reviewed (Landegren, et al., Science, 242: 229-237, 1988). To determine whether an agent can functionally complex with the Binl polypeptide, the agent is incubated and any complex formed between Binl and the agent is separated from the unbound Binl polypeptide. The agent can then be isolated from the Binl complex. Combinatorial chemistry methods are also included in the method of selection of the invention to identify chemical compounds that bind to Binl. Ligands / agents that bind to Binl can be tested in standard labeling assays. Selection methods include the inhibition of brassinosteroid or hormone binding with Binl (for example, the use of radiolabelled brassinosteroid). In this way, the selection method is also useful for identifying variants, binding or blocking agents, etc., which functionally, if not physically (eg, sterically) act as antagonists or agonists, as desired. The ligands or test agents can be detected directly or indirectly with labels, for example, with a radioisotope, a fluorescent compound, a bioluminescent compound, a quinolinescent compound, a metal chelator or an enzyme. Those skilled in the art will know of other convenient labels to bind the test agent, or will be able to find them, using routine experimentation. In addition, commonly used binding assays, such as equilibrium saturation binding assay can be used to identify binl binding and blocking agents. ANTI-SENSE INHIBITION OR RIBOZÍMA DE B ± nl The anti-sense technology offers a very specific and powerful means to provide plants that can be maintained in a vegetative state, thereby increasing biomass or seed yield. Anti-sense molecules are introduced into cells that contain Binl, for example, and work by decreasing the amount of Binl expression in a cell. Anti-sense polynucleotides in the context of the present invention include both short nucleic acid sequences known as oligonucleotides of usually 10 to 50 bases in length as well as longer nucleic acid sequences that can exceed the length of the same gene sequence Binl. The anti-sense polynucleotides useful for the present invention are complementary to specific regions of a corresponding target mRNA. Hybridization of anti-sense polynucleotides to their target transcripts can be very specific as a result of a complementary base pair. The ability of the anti-sense polynucleotides to hybridize is affected by parameters such as length, chemical modification and secondary structure of the transcript that can influence the access of the polynucleotide to the target site. See Stein et al., Cancer Research _48.:2659 (1988). An anti-sense polynucleotide can be introduced into a cell by introducing a segment of nucleic acid encoding the polynucleotide. An anti-sense polynucleotide can also be introduced into a cell by adding the polynucleotide to the environment of the cell so that the cell can directly collect the polynucleotide. The last route is preferred for shorter polynucleotides up to about 20 bases in length. To select the preferred length of a given polynucleotide, a balance must be struck to the gain of the most favorable characteristics. The shorter polynucleotides such as 10 to 15 mers, although they offer greater cellular penetration, have lower gene specificity. In contrast, although polynucleotides longer than 20 to 30 bases offer better specificity, they show a decreased absorption kinetics within the cells. See Stein et al., PHOSPHOROT-HIOATE OLIGODEOXYNUCLEOTIDE ANALOGUES in "Oligodeoxynucleotides -Antisense Inhibitors of Gene Expression" Cohen, ed. McMillan Press, London (1988). The accessibility of target sequences of mRNA is also of importance and, therefore, the regions that form cycles in the target mRNA offer promising targets. In this description the term "polynucleotide" encompasses both oligomeric nucleic acid fractions of the type-61 found in nature, such as deoxyribo-nucleotide and ribonucleotide structures of the nucleic acid and RNA, and man-made analogs that are capable of binding to nucleic acids found in nature. The polynucleotides of the present invention can be based on ribonucleotide or deoxyribonucleotide monomers linked by phosphodiester linkages, or by analogs linked by methyl phosphonate, phosphorothioate, or other linkages. They can also compromise monomer fractions that have altered base structures or other modifications, but still retain the ability to bind naturally occurring nucleic acid and RNA structures. These polynucleotides can be prepared by methods well known in the art, for example using machines and reagents commercially available from Perkin-Elmer / Applied Biosystems (Foster City, California). Phosphodiester-linked polynucleotides are particularly susceptible to the action of nucleases in serum or the interior of cells, and therefore in a preferred embodiment the polynucleotides of the present invention are linked phosphorothioate or methyl phosphonate analogues, which have been shown to be resistant to nuclease. Those of ordinary skill in this art will be able to select other links for use with this invention. These modifications can also be designed to improve cellular uptake and stability of the polynucleotides.

Polynucleotides that have the ability to hybridize with mRNA targets can inhibit the expression of the corresponding gene products by multiple mechanisms. The "arrest of the translation", the interaction of polynucleotides with target mRNA blocks the action of the ribosomal complex, and therefore, prevents translation of the messenger RNA into protein. Haeuptle and collaborators, Nucí. Acids Res. 14: 1427 (1986). In the case of phosphodiester or phosphorothioate nucleic acid polynucleotides, RNase H can digest the target RNA sequence as it has hybridized to the nucleic acid oligomer. Walder and Walder, Proc. Na ti. Acad. Sci. USA .85 .: 5011 (1988). As another mechanism of action, in the "arrest of transcription" it appears that some polynucleotides can form "triplex", or triple helix structures with double-stranded genomic nucleic acid containing the gene of interest, thereby interfering with transcription by RNA polymerase. Giovannangeli et al., Proc. Nati Acad. Sci. 90: 10013 (1993); Ebbinghaus et al., J. Clin. Invest. 92: 2433 (1993). In a preferred embodiment, Binl polynucleotides are synthesized according to standard methodology. Phosphorothioate-modified nucleic acid polynucleotides are typically synthesized in automated nucleic acid synthesizers available from a variety of manufacturers. These instruments are capable of synthesizing amounts in nanomoles of polynucleotides of as much as 100 nucleotides. The shorter polynucleotides synthesized by modern instruments are often convenient for use without further purification. If necessary, the polynucleotides can be purified by polyacrylamide gel electrophoresis or reverse phase chromatography. See Sambrook et al., MOLECULAR CLONING: A Laboratory Manual, Vol. 2, Chapter 11, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York (1989). Alternatively, a Binl polynucleotide in the form of an anti-sense RNA can be introduced into a cell by its expression within the cell from a standard nucleic acid expression vector. Binl anti-sense nucleic acid sequences can be cloned from standard plasmids into expression vectors, these expression vectors have characteristics that allow higher levels of, or more efficient expression of, resident polynucleotides. At a minimum, these constructs require a prokaryotic or eukaryotic promoter sequence which initiates the transcription of the inserted nucleic acid sequences. A preferred expression vector is one wherein the expression is inducible at high levels. This is accomplished by the addition of a regulatory region that provides for the increased transcription of downstream sequences in the appropriate host cell. See Sambrook et al., Vol. 3, Chapter 16 (1989). For example, Binl anti-sense expression vectors can be constructed using the polymerase chain reaction (PCR) to amplify suitable fragments from single-stranded cDNA of a plasmid such as pRc in which the BinL cDNA It has been incorporated. Fang et al., J. Biol. Chem. 267: 25889-25897 (1992). Polynucleotide synthesis and purification techniques are described in Sambrook et al., And Ausubel et al., (Eds.), CURRENT PROTOCOLS IN MOLECULAR BIOLOGY (Wiley Interscience 1987) (hereinafter "Ausubel"), respectively. The polymerase chain reaction procedure is carried out by well-known methodology. See, for example, Ausubel, and Bangham, "The Polymerase Chain Reaction: Getting Started," in PROTOCOLS IN HUMAN MOLECULAR GENETICS (Humana Press 1991). Furthermore, polymerase chain reaction kits can be purchased from companies such as Stratagene Cloning Systems (La Jolla, California) and Invitrogen (San Diego)., California). The products of the polymerase chain reaction are subcloned into cloning vectors. In this context a "cloning vector" is a nucleic acid molecule, such as a plasmid, cosmid or bacteriophage, which can be replicated autonomously in a host prokaryotic cell. Cloning vectors typically contain one or a small number of restriction endonuclease recognition sites in which foreign nucleic acid sequences can be inserted in a determinable manner without loss of an essential biological function of the vector, as well as a marker gene which it is suitable for use in the identification and selection of cells transformed with the cloning vector. Suitable cloning vectors are described by Sambrook et al., Ausubel, and Brown (ed.), MOLECULAR BIOLOGY LABFAX (Academic Press 1991). Cloning vectors can be obtained, for example, from GIBCO / BRL (Gaithersburg, Maryland), Clontech Laboratories, Inc.

(Palo Alto, California), Promega Corporation (Madison, Wisconsin), Stratagene Cloning Systems (La Jolla, California), Invitrogen (San Diego, California), and the American Type Culture Collection (Rockville, Maryland). Preferably the polymerase chain reaction products are linked to a "TA" cloning vector. Methods for generating polymerase chain reaction products with an overlap of thymidine or adenine are well known to those skilled in the art. See, for example, Ausubel on pages 15.7.1-15.7.6. Furthermore, games to perform TA cloning can be purchased from companies such as Invitrogen (San Diego, CA). The cloned anti-sense fragments are amplified by transforming competent bacterial cells with a cloning vector and culturing the bacterial host cells in the presence of the appropriate antibiotic. See, for example, Sambrook et al., And Ausubel. The polymerase chain reaction is then used to select bacterial host cells for Binl anti-sense orientation clones. The use of polymerase chain reaction for bacterial host cells is described, for example, by Hofmann et al., "Sequencing DNA Amplified Directly from a Bacterial Colony", in PCR PROTOCOLS: METHODS AND APPLICATIONS, White (ed.), Pages 205 -210 (Humana Press 1993), and by Cooper et al., "PCR-Based Full-Length Cloning Cloning Utilizing the Universal-Adapter / Specific DOS Primer-Pair Strategy", Id. At pages 305-316. The cloned anti-sense fragments are dissociated from the cloning vector and inserted into an expression vector. For example, Hi.nc.III and Xbai can be used to dissociate the anti-sense fragment from the TA cloning vector pCR®-II (Invitrogen, San Diego, California). Convenient expression vectors typically contain (1) prokaryotic nucleic acid elements that encode a replication bacterial origin and an antibiotic resistance marker to provide amplification and selection of the expression vector in a bacterial host; (2) nucleic acid elements that control the initiation of transcription, such as a promoter; and (3) nucleic acid elements that control the processing of transcripts, such as a transcription / polyadenylation termination sequence. For a plant host, transcriptional and translational regulatory signals are preferably derived from viral sources in which regulatory signals are associated with a particular gene that has a high level of expression. The transcriptional regulatory sequences include a promoter region sufficient to direct the initiation of RNA synthesis. Suitable promoters include those described above, for plant expression vectors (e.g., CaMV and FMV). The anti-sense polynucleotides according to the present invention are derived from any portion of the open reading frame of the Binl cDNA. Preferably, the mRNA (i) sequences surrounding the translation start site and (ii) forming cycle structures are objective. Based on the size of the human genome, statistical studies show that a nucleic acid segment of approximately 14-15 base pairs in length will have a unique sequence in the genome. To ensure the specificity of targeting the Binl RNA, therefore, it is preferred that the antisense polynucleotides be at least 15 nucleotides in length. Not all anti-sense polynucleotides will provide a sufficient degree of inhibition or a sufficient level of specificity for the goal of Binl. Thus, it will be necessary to analyze the polynucleotides to determine which one has the appropriate anti-sense characteristics. A preferred method of testing a useful anti-sense polynucleotide is the inhibition of protein kinase activity or the inhibition of a steroid bond.

The above approaches can also be used not only with anti-sense nucleic acid, but also with ribozymes, or with triplex agents to block the transcription or translation of a specific Bin1 mRNA, either by masking the mRNA with an anti-sense nucleic acid or a triplex agent, or dissociating it with a ribozyme. The use of an oligonucleotide to stop transcription is known as a triplex strategy since the oligomer becomes entangled around the double helical nucleic acid, forming a triple-stranded helix. Therefore, these triplex compounds can be designed to recognize a single site in a chosen gene (Maher, et al., Antisense Res. And Dev., 1 (3): 227, 1991; Helene, C, Anticancer Drug Design, 6 (6): 569, 1991). Ribozymes are RNA molecules that have the ability to specifically dissociate other single-stranded RNA in a manner analogous to nucleic acid restriction endonucleases. Through modification of the nucleotide sequences encoding the RNAs, it is possible to overlap molecules that recognize specific nucleotide sequences in the RNA molecule and dissociate them (Cech, J. Amer. Med. Assn., 260: 3030, 1988). . An important advantage of this approach is that, because they are sequence specific, only mRNAs with particular sequences are inactivated. There are two basic types of ribozymes namely, tetrahymena type ((Hasselhoff, Na ture, 334: 585, 1988) and "hammerhead" type. The tetrahymena-like ribozymes recognize sequences that are four bases in length, while the ribozymes type "Hammerhead" recognize base sequences of 11 to 18 bases in length.The longer the recognition sequence, the greater the probability that the sequence will occur exclusively in the target mRNA species. hammerhead ribozymes to tetrahymena-type ribozymes to inactivate a specific mRNA species and recognition sequences based on 18 are preferred over shorter recognition sequences B ± nl LIKE CONTRACEPTION Vegetable Binl homologues may play a role in the regulation of menstrual cycle or regulation of uterine function during pregnancy, and therefore, Binl, anti-Binl antibodies, or polynucleotides The anti-sense can be useful either in contraceptive regimens, to increase the success of in vitro fertilization procedures, or to prevent premature labor. The methods described herein can be used for the administration of Binl or Binl agents for these purposes. The invention also includes various pharmaceutical compositions that block the binding of brassinosteroids or hormones with Binl. The pharmaceutical compositions according to the invention are prepared by placing an antibody against Binl, a peptide or peptide derivative of Binl, a mimetic of Binl, or a binding agent of Binl according to the present invention in a convenient form for administration to a subject using carriers, excipients and additives or auxiliaries. The foregoing description generally describes the present invention. A more complete understanding can be obtained by reference to the following specific examples which are provided herein for purposes of illustration only and are not intended to limit the scope of the invention. EXAMPLES EXAMPLE 1 CLONING OF THE Binl POLYUCLEOTIDE The following protocol was used to clone the plant Binl polynucleotide. We identified 18 new dwarf Arabidopsis mutants that lacked the ability to respond to brasinolide and were called bin mutants. The binl mutations were used to map the gene in a small range of the Arabidopsis 4 chromosome. The Binl was cloned using standard methods of map-based cloning. The Binl coding polynucleotide was identified within this range by sequencing the wild-type and the mutant alleles of this nucleic acid. All the mutant DNAs contained a mutation in the Binl coding sequence whereby it was established that this interval contained the Binl gene. (See Li et al., Science 272: 398, 1996).

EXAMPLE 2 COMPARISON OF BINL WITH OTHER RECEPTOR KINASES A BLAST search was performed using the sequence of SEQ ID NO: 1. Several receptor-like and receptor-like proteins (eg, serine / threonine) having homology with Binl, were identified. both in plant species and in non-vegetable species. Some of these sequences are listed below: ERECTA (Arabidopsis) receptor kinase CLV1 (Arabidopsis) protein AWJL218 (wheat) interactor Pto kinase 1 product ARK2 protein kinase S50767 (rice) kinase putative corn receptor protein ZMP protein AWJL236 (wheat) receptor ipomoea trifid receptor associated with interleukin-1 kinase (human) Although the invention has been described with reference to the currently preferred embodiments, it should be understood that various modifications can be made without departing from the spirit of the invention. In accordance with the foregoing, the invention is limited only by the following claims.

LIST OF SEQUENCES (1) GENERAL INFORMATION: (i) APPLICANT: THE SALK INSTITUTE FOR BIOLOGICAL STUDIES (ii) TITLE OF THE INVENTION: RECEPTOR KINASE, BIN1 (iii) NUMBER OF SEQUENCES: 2 (2) INFORMATION FOR SEQ ID NO : 1: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 4104 PAIRS OF BASES (B) TYPE: NUCLEIC ACIDS (C) RANDOMITY: SINGLE (D) TOPOLOGY: LINEAR (ii) TYPE OF MOLECULE: DNA (GENOMIC) (vii) IMMEDIATE SOURCE: (B) CLONA: BIN1 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 1: CTTCCACTTC CTCTGTAATG GTGGAACCAA AACCCTAGAT TCCCCCTTTC ATCTTCTCTA 60 CTTCCCACAC TTTTCTCTCT CACAAACTCT TGAGAAATGA AGACTTTTTC AAGCTTCTTT 120 CTCTCTGTAA CAACTCTCTT CTTCTTCTCC TTCTTTTCTC TTTCATTTCA AGCTTCACCA 180 TCTCAGTCTT TATACAGAGA AATCCATCAG CTTATAAGCT TCAAAGACGT TCTTCCTGAC 240 AAGAATCTTC TCCCAGACTG GTCTTCCAAC AAA? ACCCGT GTACTTTCGA TGGCGTT? CT 300 TGCAGAGACG ACAAAGTTAC TTCGATTGAT CTCAGCTCCA AGCCTCTCAA CGTCGG? TTC 360 AGTGCCGTGT CCTCGTCTCT CCTGTCTCTC ACCGGATTAG? GTCTCTGTT TCTCTCAAAC 420 TCACACATCA ATGGCTCCGT TTCTGGCTTC AAGTGCTCTG CTTCTTTAAC CAGCTTGGAT 480 CTATCTAGAA ACTCTCTTTC GGGTCCTGTA ACGACTCTAA CAAGCCTTGG TTCTTGCTCC 540 GGTCTGAAGT TTCTTAACGT CTCTTCCAAT ACACTTGATT TTCCCGGGAA AGTTTCAGGT 600 GGGTTGAAGC TAAACAGCTT GGAAGTTCTG GATCTTTCTG CG? ATTCAAT CTCCGGTGCT 660 AACGTCGTTG GTTGGGTTCT CTCCGATGGG TGTGGAGAGT TGAAACATTT AGCGATTAGC 720 GGAAACAAAA TCAGTGGAGA CGTCGATGTT TCTCGCTGCG TGAATCTCGA GTTTCTCGAT 780 GTTTCCTCCA ACAATTTCTC CACTGGGATT CCTTTCCTCG GAGATTGCTC TGCTCTGCAA 840 CATCTTGACA TCTCCGGGAA CAAATTATCC GGCGATTTCT CCCGTGCTAT CTCTACTTGC 900 ACAGAGCTCA AGTTGTTGAA CATCTCTAGT AACCAATTCG TCGGACCAAT CCCTCCGCTA 960 CCGCTTAAAA GTCTCCAATA CCTCTCTCTG GCCGAGA? CA AATTCACCGG CGAGATCCCT 1020 GACTTTCTCT CCGGCGCG TG TGATACACTC ACTGGTCTCG ATCTCTCTGG AAATCATTTC 1080 TACGGTGCGG TTCCTCCATT CTTCGGTTCA TGTTCTCTTC TCGAATCACT CGCGTTGTCG 1140 AGTAACAACT TCTCTGGCGA GTTACCGATG GATACGTTGT TGAAGATGAG AGGACTCAAA 1200 GTACTTGATC TGTCTTTCAA CGAGTTTTCC GGCGAATTAC CGGAATCTCT GACGAATCTA 1260 TCCGCTTCGT TGCTAACGTT AGATCTCAGC TCCAACAATT TCTCCGGTCC GATTCTCCCA 1320 AATCTCTGCC AGAACCCTAA AAACACTCTG CAGGAGCTTT ACCTTCAGAA CAATGGCTTC 1380 ACCGGGAAGA TTCCACCGAC TTTAAGCAAC TGTTCTGAGC TGGTTTCGCT TCACTTGAGC 1440 TTCAATTACC TCTCCGGGAC AATCCCTTCG AGCTTAGGCT CTCTATCGAA GCTTCGAGAT 1500 CTGAAACTAT GGCTGAATAT GTTAGAAGGA GAGATCCCTC AGGAGCTCAT GTATGTCAAG 1560 ACCTTAGAGA CTCTGATCCT CGACTTCAAC GATTTAACCG GTGAAATCCC TTCCGGTTTA 1620 AGTAACTGTA CCAATCTTAA CTGGATTTCT CTGTCGAATA ACCGGTTAAC CGGTGAGATT 1680 CCGAAATGGA TTGGCCGGTT AGAGAATCTC GCTATCCTCA AGTTAAGCAA CAATTCATTC 1740 TCCGGGAACA TTCCGGATGA GCTCGGCGAC TGCAG? AGCT TAATCTGGCT TGATCTCAAC 1800 ACCAATCTCT TCAATGGAAC GATTCCGGCG GCGATGTTTA AACAATCCGG GAAAATCGCT 1860 GCCAATTTCA TCGCCGGTAA GAG GTACGTT TATATCAAAA ACGATGGGAT GAAGAAAGAG 1920 TGTCATGGAG CTGGTAATTT ACTTGAGTTT CAAGGAATCA GATCCGAACA ATTAAACCGG 1980 CTTTCAACGA GGAACCCTTG TAATATCACT AGCAGAGTCT ATGGAGGTCA CACTTCGCCG 2040 ACGTTTGATA ACAATGGTTC GATGATGTTT CTGGACATGT CTTACAACAT GTTGTCTGGA 2100 TACATACCGA AGGAGATTGG TTCGATGCCT TATCTGTTTA TTCTCAATTT GGGTCATAAC 2160 GATATCTCTG GTTCGATTCC TGATGAGGTA GGTGATCTAA GAGGTTTAA? CATTCTTGAT 2220 CTTTCAAGCA ATAAGCTCGA TGGGAGGATT CCTCAGGCTA TGTCAGCTCT TACTATGCTT 2280 ACGGAAATCG ATTTGTCGAA TAATAATTTG TCTGGTCCGA TTCCTGAGAT GGGTCAGTTT 2340 GAGACTTTTC CACCGGCTAA GTTCTTGAAC AATCCTGGTC TCTGTGGTTA TCCTCTTCCG 2400 CGGTGTGATC CTTCAAATGC AGACGGTTAT GCTCATCATC AGAGATCTCA TGGAAGGAGA 2460 CCAGCGTCCC TTGCTGGTAG TGTGGCGATG GGATTGTTGT TCTCTTTTGT GTGTATATTT 2520 GGGCTGATCC TTGTTGGTAG AGAGATGAGG AAGAGACGGA GAAAGAAAGA GGCGGAGTTG 2580 GAGATGTATG CGGAAGGACA TGGAAACTCT GGCGATAGAA CTGCTAACAA CACCAATTGG 2640 AAGCTGACTG GTGTGAAAGA AGCCTTGAGT ATCAATCTTG CTGCTTTCGA GAAGCCATTG 2700 CGGAAGCTCA CGTTTGCGGA TCTTCTTCAG GCTACCAATG GTTTCCATAA TGATAGTCTG 2760 ATTGGTTCTG GTGGGTTTGG AGATGTTTAC AAAGCGATTT TGAAAGATGG AAGCGCGGTG 2820 GCTATCAAGA AACTGATTCA TGTTAGCGGT CAAGGTGATA GAGAGTTCAT GGCGGAGATG 2880 GAAACCATTG GGAAGATCAA ACATCGAAAT CTTGTGCCTC TTCTTGGTTA TTGCAAAGTT 2940 GGAGACGAGC GGCTTCTTGT TAATGAGGTT ATGAAGTATG GAAGTTTAGA AGATGTTTTG 3000 CAAGACCCCA AGAAAGGTGG GGTGAAACTT AAATTGTCCA CACGGCGGAA GATTGC GATA 3060 GGATCAGCTA GAGGGCTTGC TTTCCTTCAC CACAACTGCA GTCCGCATAT CATCCACAGA 3120 GACATGAAAT CCAGTAATGT GTTGCTTGAT GAGAATTTGG AAGCTCGGGT TTCAGATTTT 3180 GGCATGGCGA GGCTGATGAG TGCGATGGAT ACGCATTTAA GCGTCAGTAC ATTAGCTGGT 3240 ACACCGGGTT ACGTTCCTCC AGAGTATTAC CAAAGTTTCA GGTGTTCAAC AAAAGGAGAC 3300 GTTTATAGTT ACGGTGTGGT CTTACTCGAG CTACTCACGG GTAAACGGCC AACGGATTCA 3360 CCGGATTTTG GAGATAACAA CCTTGTTGGA TGGGTGAAAC AGCACGCAAA ACTGCGGATT 3420 AGCGATGTGT TTGACCCGGA GCTTATGAAG GAAGATCCAG CATTAGAGAT CGAACTTTTA 3480 CAACATTTAA AAGTTGCGGT TGCGTGTTTG GATGATCGGG CTTGGAGACG ACCGACAATG 3540 GTACAAGTCA TGGCCATGTT TAAGGAGATA CAAGCCGGGT CAGGGATAGA TTCACAGTCA 3600 ACGATCAGAT CAATAGAGGA TGGAGGGTTC AGTACAATAG AGATGGTTGA TATGAGTATA 3660 AAAGAAGTTC CTGAAGGAAA ATTATGAGAG TTAGAAACAG AGCCAAAGCA GATTCTTTGA 3720 ACATCAAAAT CATCTAAGGG TCAGTCCGAT TTTCCTTGGG TCTATTTTTT TTGTATTTTC 3780 TACTATATGC TAAGTGTATG TATCTATGTT ATTTATACAT AAGACGGATG TTTTTTTTTT 3840 CGGGCTCGGT CGAATTGGGG GTGGTGGAGA ATAGAACTAA GTAATAACTT TGTTAAGAAT 3 900 ATGTAAATAT ACAGTTTTTT GGGGAGGGAT TTGTAATGTT TTCGTTTTTA GTTCTATGGA 3960 AATTTCTACG TTGCTAACAA ATTAAATTTA TAATGAATCA TGAAGAAACA AAGAGCCAAT 4020 GTGTATTAAA TTTCGACTGA TCATGTTCAT GTAAATGCAC GTGACCTATT AATTCATTAT 4080 TGTCGGAATT AATTTGGGGA ATTC (2) INFORMATION FOR SEQ ID NO: 2: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1196 AMINO ACIDS (B) TYPE: AMINO ACIDS (D) TOPOLOGY: LINEAR (ü) TYPE OF MOLECULE: PROTEIN (vii) IMMEDIATE SOURCE: (B) CLONE: BIN1 (i) DESCRIPTION OF SEQUENCE: SEQ ID NO: 2: MKTFSSFFLSVTTLFFFSFFSLSFQASPSQSLYREIHQLISF. ? VLPDKNLLPDWSSNKNPCTFDGVT 'CRDDKVTSIDLSSKPLNVGFSAVSSSLLSLTGLESLFLSNSHINGSVSGFKCSASLTSLDLSRNSL? G PVTTLTSLGSCSGLKFLNVSSNTLDFPG VSGGLKLNSLEVLDLSANSISGANWG VLSDGCGEL KHLAISGNKISGDVDVSRCV_.LEFLDVSSNNFSTGIPFLGDCSA_.QHIiDISGNKI_SGDFSRAISTCTELKI.LNIS SNQFVGPIPPLPLKSLQYLSLAENKFTGEIPDFLSGACDTLTGLDLSGNHFYGAVPPFFGSCSLLESLALSSNNF SGELPMDTLLK RGLKVLDLSFNEFSGELPESLTNLSASLLTLDI.SSNNFSGPILPNLCQNPKNTLQE LYLQNNGFTGKIPPTLSNCSELVSLHLSFNYLSGT IPSSLGSLSKLRDLKL LNMLEGEIPQELMYVKTLETLIL DFNDLTGEIPSGLSNCTNLNWISLSNNRLTGEIPKWIGRLENLAILKLSNNSFSGNIPDELGDCRSLIWLDLNTN LFNGT1PAAMFKQSGKIAANFIAGKRYVYIKNDGMKKECHGAGNLLEFQGIRSEQLNRLSTRNPCNITSRVYGGH TSPTFDNNGSMMFLDMS NMLSGYIPKEIGSMPYLFILNLGHNDISGSIPDEVGDLRGLNILDLSSNKLDGRIPQ AMSALTMLTEIDLSNNNLSGPIPE GQFETFPPAKFLNNPGLCGYPLPRCDPSNADGYAHHQRSHGRRPASLAGS VAMGLLFSFVCIFGLILVGREMRKRRRKKEAELEMYAEGHGNSGDRTANNTNWKLTGVKEALSINLAAFEKPLRK LTFADLLQATNGFHNDSLIGSGGFGDVYKAILKDGSAVAIKKLIHVSGQGDREFMAEMETIGKIKHRNLVPLLGY CKVGDERLLVNEVMKYGSLEDVLQDPKKGGVKLKLSTRRKIAIGSARGLAFLHHNCSPHIIHRDMKSSNVLLDEN LEARVSDFGMARLMSAMDTHLSVSTLAGTPGYVPPEYYQSFRCSTKGDVYSYGWLLELLTGKRPTDSPDFGDNN LVG VKQHAKLRISDVFDPELMKEDPALEIELLQHLKVAVACLDDRAWRRPTMVQVMAMFKEIQAGSGIDSQSTI RSIEDGGFSTIEMVDMSIKEVPEGKL

Claims (67)

1. CLAIMS 1. Binl polypeptide substantially purified. 2. The polypeptide according to claim 1, characterized by: a) having a molecular weight of about 130 kD, as determined by SDS-PAGE; b) have receptor kinase activity; and c) operate in the brasinolide response path. 3. The polypeptide according to claim 1, wherein the amino acid sequence of said protein is substantially the same as the amino acid sequence set forth in SEQ. ID. DO NOT. 2 (figure 1). 4. The polypeptide according to claim 1, wherein the amino acid sequence is that established in SEQ. ID. DO NOT. 2 (figure 1). 5. The polypeptide of claim 3, wherein the amino acid residue 611 is changed from glycine to glutamic acid. 6. A peptide having an amino acid sequence around amino acid residue 588 to 649 of SEQ. ID. DO NOT. 2, where the peptide is linked to brassinosteroids. 7. An isolated polynucleotide encoding the Bin1 polypeptide of claim 1. 8. An isolated polynucleotide selected from the group consisting of: a) SEQ. ID. DO NOT . 1; b) SEQ. ID. DO NOT. 1, where T can also be U; c) Nucleic acid sequences complementary to SEQ. ID. DO NOT. 1; and d) fragments of a), b) and c) that are at least 15 bases in length and that will hybridize to the genomic nucleic acid encoding the SEQ protein. ID. DO NOT.
2. 2. The polynucleotide of claim 7, wherein the polynucleotide is isolated from a plant cell. 10. The polynucleotide of claim 7, wherein the polynucleotide is isolated from a mammalian cell. 11. A recombinant expression vector comprising a polynucleotide sequence according to claim 7. 12. A host cell containing the vector of claim 11. 13. An antibody that binds to the protein of claim 1, or it is linked to antigenic fragments of said protein. 14. A method of producing a genetically modified plant, characterized by having an increased yield compared to a wild-type plant, said method comprising: introducing at least one nucleic acid sequence encoding the Binl polypeptide into a plant cell to obtain nna transformed plant cell, said nucleic acid sequence operably associated with a promoter; producing a plant from said transformed plant cell under conditions that allow expression of the Binl polypeptide; and selecting a plant exhibiting said increased yield. 15. The method of claim 14, wherein said introduction is by physical means. 16. The method of claim 14, wherein said introduction is by chemical means. The method of claim 14, wherein the plant cell is selected from the group consisting of protoplasts, gamete-producing cells, and cells that are regenerated into whole plants. 18. The method of claim 14, wherein the promoter is selected from the group consisting of a constitutive promoter and an inducible promoter. 19. A plant produced by the method of claim 14. 20. Plant tissue derived from a plant produced by the method of claim 14. 21. A seed derived from a plant produced by the method of claim 14. 22. A method for genetically modifying a plant cell such that a plant, produced from said cell, is characterized as having a modulated yield as compared to a wild-type plant, said method comprising: introducing the polynucleotide encoding Binl of claim 7 in a plant cell to obtain a transformed plant cell; and culturing the transformed plant cell under conditions that allow the modulation of the Binl polypeptide, thereby producing a plant having modulated yield. 23. The method of claim 22, wherein said modulated performance is increased yield. The method of claim 22, wherein said modulated performance is reduced throughput. 25. The method of claim 23, wherein said increased yield is achieved by inducing the expression of binl in the plant. 26. The method of claim 23, wherein said increased yield is achieved by increasing the expression of binl in the plant. 27. A method of producing a plant characterized by having an increased yield compared to a wild-type plant, said method comprising: contacting a susceptible plant with an inducing amount of the binl promoter of an agent necessary to elevate the expression of the binl gene. about the expression of binl in a plant not in contact with the agent. 28. The method of claim 27, wherein the agent is a transcription factor. 29. The method of claim 27, wherein the agent is a chemical agent. 30. The method of claim 27, wherein said increased yield is increased vegetative biomass. 31. The method of claim 30, wherein the agent is an anti-sense molecule. 32. A recombinant cell line expressing the Binl polypeptide. 33. A substantially purified fragment of the Bin1 polypeptide, wherein said fragment inhibits the binding of brassinosteroids to the Bin1 polypeptide. 34. A substantially purified Binl ligation agent, wherein said ligation agent inhibits the binding of brassinosteroids to the Binl polypeptide. 35. The agent of claim 34, wherein said agent is selected from a biological agent and a chemical compound. 36. The agent as in claim 34, wherein said agent is an anti-Binl antibody or epitope ligation fragment thereof. 37. A method for inhibiting the binding of brasinoeste-roids to a Binl polypeptide, which comprises contacting the Bin1 polypeptide with an anti-Binl antibody. 38. The method of claim 37, wherein said contacting is by in vivo administration to a host subject. 39. The method of claim 38, wherein said anti-Binl antibody is administered by intravenous, intramuscular or subcutaneous injection. 40. The method of claim 38, wherein said antibody is formulated in a pharmaceutically acceptable carrier. 41. A method for identifying a binl polypeptide binding agent, comprising: a) incubating the Binl polypeptide or a cell expressing the Binl polypeptide and a suspected binding agent; b) separating a complex from the Bin1 polypeptide and said unbound ligand of Bin1 polypeptide; and c) isolating the agent. 42. A method for identifying an agent that binds to the Bin1 polypeptide, comprising: a) incubating said agent and Bin1 polypeptide under conditions sufficient to allow the agent and the Bin1 polypeptide to form a complex; b) separating a Binl polypeptide complex and said unlinked Binl polypeptide binding agent; and c) measuring the ligation or ligation effect of the composition to the Binl polypeptide. 43. The method of claim 42, wherein said composition is selected from a small molecule selected from the group consisting of a steroid and a growth regulator. 44. The method of claim 43, wherein said composition is a peptide. 45. The method of claim 43, wherein said composition is a peptidomimetic. 46. The method of claim 42, wherein said Bin1 polypeptide is a cell surface polypeptide. 47. The method of claim 42, wherein the measurement of the ability of the composition to bind the Bin1 polypeptide is detected by reporter means. 48. The method of claim 47, wherein said reporter means is selected from the group consisting of a radioisotope, a fluorescent compound, a bioluminescent compound, a chemiluminescent compound, a metal chelator, or an enzyme. 49. A method of producing genetically transformed disease-resistant plants, comprising: a) introducing the genome of a plant cell, to obtain a transformed plant cell, a nucleic acid construct comprising: (i) a promoter that it works in plant cells to cause the production of an RNA sequence; and (ii) a nucleic acid coding sequence encoding the Bin1 polypeptide; and b) regenerating from the transformed plant cells genetically transformed plants expressing the Binl polypeptide in an amount effective to inhibit infection by a bacterial or fungal pathogen. 50. The method of claim 49, wherein said nucleic acid sequence is SEQ. ID. DO NOT. 1. The method of claim 49, wherein said promoter is selected from the FMV35S and CaMV35S promoters. 52. The method of claim 49, wherein said promoter is induced by pathogen infection. 53. A genetically transformed, disease-resistant plant comprising a recombinant nucleic acid sequence containing in operable linkage: a) a promoter that functions in plant cells to cause the production of an RNA sequence; and b) a structural coding sequence encoding the Bin1 polypeptide. 54. The plant of claim 53, wherein said promoter is selected from the FMV35S and CaMV35S promoters. 55. The plant of claim 53, wherein said promoter is induced by pathogen infection. 56. The plant of claim 53, wherein said structural coding sequence is SEQ. ID. DO NOT. 1. 57. A non-human, transgenic animal having a phenotype characterized by expression of the Bin1 polypeptide, the phenotype being conferred by a transgene contained in the somatic and germinal cells of the animal, the transgene comprising a nucleic acid sequence encoding the Binl polypeptide. 58. A method for producing a non-human, transgenic animal having a phenotype characterized by expression of the Binl polypeptide not normally expressed in the animal in another way, the method comprising: a) introducing at least one transgene into a zygote of an animal, the transgene (s) comprising a nucleic acid construct encoding the Binl receptor, b) transplanting the zygote to a pseudo-pregnant animal, c) allowing the zygote to develop at term, and d) identifying at least one transgenic product containing the transgene. 59. A non-human, transgenic animal that has a transgene that disturbs or interferes with the expression of the Binl polypeptide chromosomally integrated into the germ cells of the animal. 60. The non-human, transgenic animal of claim 59, wherein the transgene comprises the Binl anti-sense polynucleotide. 61. A method for inhibiting the expression of the Binl polypeptide in a cell, comprising contacting Bin1 polypeptide with an effective inhibitory amount of an anti-sense oligonucleotide that is linked to a segment of a mRNA transcribed from a polypeptide gene Binl, whereby the antisense binding to the mRNA fragment 62. A method for stimulating oocyte maturation, comprising contacting oocytes with an effective amount of the Binl polypeptide, as set forth in SEQ. ID. DO NOT. 2, thereby increasing the maturation rate of oocytes compared to untreated oocytes. 63. The method of claim 62, wherein the contact is in vitro. 64. The method of claim 62, wherein the contact is in vivo. 65. A method for inhibiting oocyte maturation, comprising contacting oocytes with an inhibitor of the Binl polypeptide, thereby inhibiting oocyte maturation as compared to untreated oocytes. 66. The method of claim 65, wherein the inhibitor is a Binl anti-sense molecule. 67. The method of claim 65, wherein the inhibitor is a Binl antibody.