Archaea are distinct from both Bacteria and Eukaryotes, earning them their own domain in the Three Domain Classification originally proposed by Woese in 1977, alongside the Eukarya and the Bacteria.
Archaea can survive in
extreme environments, such as places high in acid, salt, or heat, earning them the name “extremophiles,”
https://open.oregonstate.education/generalmicrobiology/chapter/archaea/ Specific Characteristics in Archaea cellular membranes
Top, an archaeal phospholipid:
1, isoprene chains; 2, ether linkages; 3, L-glycerol moiety; 4, phosphate group. Middle, a bacterial or eukaryotic phospholipid: 5, fatty acid chains; 6, ester linkages; 7, D-glycerol moiety; 8, phosphate group. Bottom: 9, lipid bilayer of bacteria and eukaryotes; 10, lipid monolayer of some archaea
ARCHAEA Morphology, Physiology, biochemistry, diversity & Industrial Applications of domain Archaea, 2015 Major lipids of Archaea and the architecture of archaeal membranes
Note that the hydrocarbon of the
lipid is bonded to the glycerol by an ether linkage in both cases. The hydrocarbon is phytanyl (C20) in part a and biphytanyl (C40) in part b. (c) A major lipid of Thaumarchaeota is crenarchaeol, a lipid containing 5- and 6-carbon rings.
ARCHAEA Morphology, Physiology, biochemistry, diversity & Industrial Applications of domain Archaea, 2015 Major lipids of Archaea and the architecture of archaeal membranes
Membrane structure in Archaea may be bilayer or monolayer (or a mix of both).
ARCHAEA Morphology, Physiology, biochemistry, diversity & Industrial Applications of domain Archaea, 2015 What is membrane curvature?
Membranes need to be bent to impart a shape to cells,
internal organelles, and vesicles. Bending of membranes is a requisite for the formation of spherical vesicles, which are critical components of membrane trafficking, and for changes in cell shape during cell migration and cell death
Peripheral membrane scaffolding membranes such as
BAR (Bin-Amphiphysin-Rvs) domains, which are banana-shaped and bind preferentially to concave membrane surfaces that are negatively-charged and function as a curvature-sensing protein.
Membrane bending during lamellipodia
and filopodia extensions, mitotic cell rounding and maintenance of membrane curvature within internal organelles like golgi and endoplasmic reticulum are all mediated by the cytoskeleton.
https://www.mechanobio.info/what-is-the-plasma-membrane/what-is-membrane-curvature/ Spontaneous membrane curvature Phospholipid form
Type I lipids such as phosphatidylinositol or modified forms of
DOPC where one fatty acid residue is removed, for example lyso- PC, which have larger head groups relative to their long fatty acid chains lead to cone-shaped structure, inducing negative curvature.
Type 0 lipids such as phosphatidylcholines (PC), and
phosphatidylserine (PS), which are Cylindrical in shape prefer no curvature and often form flat bilayers
Due to smaller headgroups compared to their wider fatty acid
chains, type II lipids such as phosphatidylethanolamine (PE) prefer negative curvature. Lipids like phosphatidyl ethanolamine (PtdEtn) have a smaller head group to acyl chain ratio, and therefore have a conical shape. As the head groups of PtdEtn lipid clusters come closer together, the broader acyl bases impose a positive curvature on the membrane. dx.doi.org/10.1021/bi301332v | Biochemistry 2012, 51, 9782−9795 Proteins with amphipathic helices insert into bilayers to induce positive curvature
For example, epsin is a protein involved in clathrin-coated
pit formation in endocytosis that helps to drive membrane curvature by the insertion of its amphipathic helix
Coat proteins such as clathrin, COPI and COPII can
influence membrane bending by polymerizing into curved structures. Membrane Proteins Can Be Associated with the Lipid Bilayer in Various Ways
entirely exposed at the
external cell surface, GPI anchor transmembrane proteins (1-3) located entirely in the cytosol (4,5)
peripheral membrane protein
(7,8)
(1) a single α helix, (2) as multiple α helices, or (3) as a rolled-up β sheet (a β barrel), (4) Some of these are anchored to the cytosolic surface by an amphiphilic α helix, (5) Others are attached to the bilayer solely by a covalently bound lipid chain, (6) via an oligosaccharide linker, to phosphatidylinositol in the noncytosolic monolayer—called a GPI anchor, Lipid Anchors Control the Membrane Localization of Some Signaling Proteins
Src family of cytoplasmic protein tyrosine kinases
a saturated 14-carbon fatty acid a saturated 16-carbon fatty acid
(A) A fatty acid chain (myristic acid) is attached via an amide linkage to an N-terminal glycine. (B) A fatty acid chain (palmitic acid) is attached via a thioester linkage to a cysteine. (C) A prenyl chain (either farnesyl or a longer geranylgeranyl chain) is attached via a thioether linkage to a cysteine residue that is initially located four residues from the protein’s C-terminus. In Most Transmembrane Proteins, the Polypeptide Chain Crosses the Lipid Bilayer in an α- Helical Conformation
The free energy needed to transfer successive segments of a
polypeptide chain from a nonpolar solvent to water is calculated from the amino acid composition of each segment using data obtained from model compounds. Some β Barrels Form Large Channels
The porins are well-studied examples (example 3 in Figure 10– The FepA protein is a more complex example of a 23C). Many porin barrels are formed from a 16-strand, β barrel transport protein. It transports iron ions antiparallel β sheet rolled up into a cylindrical structure. across the bacterial outer membrane. Membrane Proteins Can Be Solubilized and Purified in Detergents Membrane Proteins Can Be Solubilized and Purified in Detergents Membrane Proteins Can Be Solubilized and Purified in Detergents Model of a membrane protein reconstituted into a nanodisc Many Membrane Proteins Diffuse in the Plane of the Membrane Many Membrane Proteins Diffuse in the Plane of the Membrane
