C-terminal domain phosphatase sensitivity of RNA polymerase II in early elongation complexes on the HIV-1 and adenovirus 2 major late templates (Q28143301)

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scientific article (publication date: 20 October 2000)

Language	Label	Description	Also known as
English	C-terminal domain phosphatase sensitivity of RNA polymerase II in early elongation complexes on the HIV-1 and adenovirus 2 major late templates	scientific article (publication date: 20 October 2000)

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scholarly article

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C-terminal domain phosphatase sensitivity of RNA polymerase II in early elongation complexes on the HIV-1 and adenovirus 2 major late templates (English)

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author name string

N F Marshall

1

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M E Dahmus

2

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language of work or name

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publication date

20 October 2000

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Journal of Biological Chemistry

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275

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42

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32430-7

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Purification of P-TEFb, a transcription factor required for the transition into productive elongation.

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Drosophila factor 2, an RNA polymerase II transcript release factor, has DNA-dependent ATPase activity.

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Purification of an RNA polymerase II transcript release factor from Drosophila

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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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Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro

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Temporal regulation of RNA polymerase II by Srb10 and Kin28 cyclin-dependent kinases

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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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Purification and characterization of an RNA polymerase II phosphatase from yeast

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

1 reference

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

1 reference

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Regulation of carboxyl-terminal domain phosphatase by HIV-1 tat protein

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Taking a new TAK on tat transactivation

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HIV-1 auxiliary proteins: making connections in a dying cell

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

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Requirements for RNA polymerase II carboxyl-terminal domain for activated transcription of human retroviruses human T-cell lymphotropic virus I and HIV-1

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Trans-activation by human immunodeficiency virus Tat protein requires the C-terminal domain of RNA polymerase II

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

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

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

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Specific interaction of Tat with the human but not rodent P-TEFb complex mediates the species-specific Tat activation of HIV-1 transcription

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Identification of a cyclin subunit required for the function of Drosophila P-TEFb

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Identification of multiple cyclin subunits of human P-TEFb

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Requirement for a kinase-specific chaperone pathway in the production of a Cdk9/cyclin T1 heterodimer responsible for P-TEFb-mediated tat stimulation of HIV-1 transcription

1 reference

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Transcription elongation factor P-TEFb mediates Tat activation of HIV-1 transcription at multiple stages

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Purification of a Tat-associated kinase reveals a TFIIH complex that modulates HIV-1 transcription

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Tat activates human immunodeficiency virus type 1 transcriptional elongation independent of TFIIH kinase

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FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO

1 reference

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A protein phosphatase functions to recycle RNA polymerase II

1 reference

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

1 reference

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Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei

1 reference

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Control of RNA initiation and elongation at the HIV-1 promoter

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The HIV-1 inducer of short transcripts activates the synthesis of 5,6-dichloro-1-beta-D-benzimidazole-resistant short transcripts in vitro.

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HIV-1 Tat overcomes inefficient transcriptional elongation in vitro

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Anti-termination of transcription within the long terminal repeat of HIV-1 by tat gene product

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Structural arrangements of transcription control domains within the 5'-untranslated leader regions of the HIV-1 and HIV-2 promoters

1 reference

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A human RNA polymerase II transcription termination factor is a SWI2/SNF2 family member

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FBI-1, a factor that binds to the HIV-1 inducer of short transcripts (IST), is a POZ domain protein

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Purification and characterization of FBI-1, a cellular factor that binds to the human immunodeficiency virus type 1 inducer of short transcripts.

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

1 reference

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Recruitment of cyclin T1/P-TEFb to an HIV type 1 long terminal repeat promoter proximal RNA target is both necessary and sufficient for full activation of transcription

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

1 reference

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10.1074/JBC.M005898200

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