(Q41735770)

8 October 2017

title

The sensitivity of RNA polymerase II in elongation complexes to C-terminal domain phosphatase (English)

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8 October 2017

A L Lehman

1

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8 October 2017

M E Dahmus

series ordinal

2

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8 October 2017

language of work or name

English

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publication date

1 May 2000

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Journal of Biological Chemistry

8 October 2017

published in

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8 October 2017

volume

275

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8 October 2017

issue

20

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8 October 2017

page(s)

14923-14932

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Genetics of transcriptional regulation in yeast: connections to the RNA polymerase II CTD.

8 October 2017

cites work

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An essential component of a C-terminal domain phosphatase that interacts with transcription factor IIF in Saccharomyces cerevisiae

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A protein phosphatase functions to recycle RNA polymerase II

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Structural changes in the RNA polymerase II transcription complex during transition from initiation to elongation

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Control of RNA polymerase II elongation potential by a novel carboxyl-terminal domain kinase

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DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs

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NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation

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Transcription elongation factor P-TEFb is required for HIV-1 tat transactivation in vitro

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Viral transactivators specifically target distinct cellular protein kinases that phosphorylate the RNA polymerase II C-terminal domain

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Purification using polyethylenimine precipitation and low molecular weight subunit analyses of calf thymus and wheat germ DNA-dependent RNA polymerase II

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Identification of a decay in transcription potential that results in elongation factor dependence of RNA polymerase II.

21 January 2018

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Dynamic interaction between a Drosophila transcription factor and RNA polymerase II.

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Dual roles for transcription factor IIF in promoter escape by RNA polymerase II.

21 January 2018

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Control of formation of two distinct classes of RNA polymerase II elongation complexes.

21 January 2018

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

21 January 2018

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Pre-mRNA processing and the CTD of RNA polymerase II: the tail that wags the dog?

21 January 2018

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P-TEFb kinase is required for HIV Tat transcriptional activation in vivo and in vitro

21 January 2018

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TAK, an HIV Tat-associated kinase, is a member of the cyclin-dependent family of protein kinases and is induced by activation of peripheral blood lymphocytes and differentiation of promonocytic cell lines

21 January 2018

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HIV-1 Tat acts as a processivity factor in vitro in conjunction with cellular elongation factors

21 January 2018

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HIV-1 Tat protein increases transcriptional initiation and stabilizes elongation

21 January 2018

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Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain

21 January 2018

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Elongator, a Multisubunit Component of a Novel RNA Polymerase II Holoenzyme for Transcriptional Elongation

21 January 2018

1 reference

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Human general transcription factor IIH phosphorylates the C-terminal domain of RNA polymerase II

21 January 2018

1 reference

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The activity of COOH-terminal domain phosphatase is regulated by a docking site on RNA polymerase II and by the general transcription factors IIF and IIB

21 January 2018

1 reference

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Mechanism of Action of RNA Polymerase II Elongation Factor Elongin

21 January 2018

1 reference

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21 January 2018

Identifiers

DOI

10.1074/JBC.275.20.14923

1 reference

8 October 2017

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