Tat stimulates cotranscriptional capping of HIV mRNA. (Q34156984)

31 July 2017

title

Tat stimulates cotranscriptional capping of HIV mRNA. (English)

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31 July 2017

Beate Schwer

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31 July 2017

Stewart Shuman

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31 July 2017

Ya-Lin Chiu

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31 July 2017

C Kiong Ho

series ordinal

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31 July 2017

Nayanendu Saha

series ordinal

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31 July 2017

Tariq M Rana

series ordinal

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31 July 2017

publication date

1 September 2002

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31 July 2017

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31 July 2017

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31 July 2017

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31 July 2017

page(s)

585-597

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HIV-1 Tat protein interacts with mammalian capping enzyme and stimulates capping of TAR RNA.

31 July 2017

cites work

1 reference

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7 January 2021

mRNA capping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxy-terminal domain

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7 January 2021

Opposing effects of Ctk1 kinase and Fcp1 phosphatase at Ser 2 of the RNA polymerase II C-terminal domain

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7 January 2021

Promoter-proximal pausing by RNA polymerase II in vitro: transcripts shorter than 20 nucleotides are not capped

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7 January 2021

Factor-dependent release of nascent RNA by ternary complexes of vaccinia RNA polymerase

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An efficient strategy to isolate full-length cDNAs based on an mRNA cap retention procedure (CAPture).

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A freeze-frame view of eukaryotic transcription during elongation and capping of nascent mRNA

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7 January 2021

Characterization of the CTD phosphatase Fcp1 from fission yeast. Preferential dephosphorylation of serine 2 versus serine 5.

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7 January 2021

Distinct roles for CTD Ser-2 and Ser-5 phosphorylation in the recruitment and allosteric activation of mammalian mRNA capping enzyme

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7 January 2021

The guanylyltransferase domain of mammalian mRNA capping enzyme binds to the phosphorylated carboxyl-terminal domain of RNA polymerase II

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7 January 2021

Human immunodeficiency virus type-1 Tat is an integral component of the activated transcription-elongation complex

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7 January 2021

Different phosphorylated forms of RNA polymerase II and associated mRNA processing factors during transcription

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7 January 2021

5'-Capping enzymes are targeted to pre-mRNA by binding to the phosphorylated carboxy-terminal domain of RNA polymerase II

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7 January 2021

Interactions between fission yeast mRNA capping enzymes and elongation factor Spt5.

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The length, phosphorylation state, and primary structure of the RNA polymerase II carboxyl-terminal domain dictate interactions with mRNA capping enzymes.

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7 January 2021

Recombinant human mRNA cap methyltransferase binds capping enzyme/RNA polymerase IIo complexes

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7 January 2021

Tat-associated kinase (P-TEFb): a component of transcription preinitiation and elongation complexes

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7 January 2021

DSIF and NELF interact with RNA polymerase II elongation complex and HIV-1 Tat stimulates P-TEFb-mediated phosphorylation of RNA polymerase II and DSIF during transcription elongation

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7 January 2021

P-TEFb, a cyclin-dependent kinase controlling elongation by RNA polymerase II

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7 January 2021

In vivo transcriptional pausing and cap formation on three Drosophila heat shock genes

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7 January 2021

Kin28, the TFIIH-associated carboxy-terminal domain kinase, facilitates the recruitment of mRNA processing machinery to RNA polymerase II.

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Characterization of human, Schizosaccharomyces pombe, and Candida albicans mRNA cap methyltransferases and complete replacement of the yeast capping apparatus by mammalian enzymes

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7 January 2021

Dynamic association of capping enzymes with transcribing RNA polymerase II

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7 January 2021

A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA

1 reference

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7 January 2021

Transcription elongation factor hSPT5 stimulates mRNA capping

1 reference

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7 January 2021

Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II

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7 January 2021

A bimolecular mechanism of HIV-1 Tat protein interaction with RNA polymerase II transcription elongation complexes

1 reference

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7 January 2021

10.1016/S1097-2765(02)00630-5

Identifiers

DOI

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31 July 2017

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