Activation of integrated provirus requires histone acetyltransferase. p300 and P/CAF are coactivators for HIV-1 Tat (Q28282041)

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H Xiao

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V V Ogryzko

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B H Howard

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Y Nakatani

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K T Jeang

Journal of Biological Chemistry

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language of work or name

English

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publication date

18 September 1998

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published in

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volume

273

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issue

38

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page(s)

24898-905

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cites work

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Role of CBP/P300 in nuclear receptor signalling

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A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors

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Nuclear protein CBP is a coactivator for the transcription factor CREB

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Activation of cAMP and mitogen responsive genes relies on a common nuclear factor

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Human p300 protein is a coactivator for the transcription factor MyoD

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Relief of YY1 transcriptional repression by adenovirus E1A is mediated by E1A-associated protein p300

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Regulation of NF-kappaB by cyclin-dependent kinases associated with the p300 coactivator

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Recruitment of p300/CBP in p53-dependent signal pathways

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A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A

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Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300

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The transcriptional coactivators p300 and CBP are histone acetyltransferases

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The CBP co-activator is a histone acetyltransferase

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Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat

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Does HIV-1 Tat induce a change in viral initiation rights?

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

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Direct interaction of human TFIID with the HIV-1 transactivator tat

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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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The type 1 human immunodeficiency virus Tat binding protein is a transcriptional activator belonging to an additional family of evolutionarily conserved genes

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Cloning of an intrinsic human TFIID subunit that interacts with multiple transcriptional activators

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Identification of a cellular protein that specifically interacts with the essential cysteine region of the HIV-1 Tat transactivator

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The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme

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

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

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Specific binding of RNA polymerase II to the human immunodeficiency virus trans-activating region RNA is regulated by cellular cofactors and Tat

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Human immunodeficiency virus type 1 and 2 Tat proteins specifically interact with RNA polymerase II.

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Repression and activation by multiprotein complexes that alter chromatin structure

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Nucleosome displacement in transcription

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Nucleosomes, DNA-binding proteins, and DNA sequence modulate retroviral integration target site selection

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Human immunodeficiency virus integrase directs integration to sites of severe DNA distortion within the nucleosome core

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Tat is required for efficient HIV-1 reverse transcription

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The role of Tat in the human immunodeficiency virus life cycle indicates a primary effect on transcriptional elongation

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Transfer of Tat and release of TAR RNA during the activation of the human immunodeficiency virus type-1 transcription elongation complex

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Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes

21 January 2018

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RNA Helicase A Mediates Association of CBP with RNA Polymerase II

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Adaptor-mediated recruitment of RNA polymerase II to a signal-dependent activator

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A growing coactivator network

21 January 2018

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A family of transcriptional adaptor proteins targeted by the E1A oncoprotein

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Adenoviral ElA-associated protein p300 as a functional homologue of the transcriptional co-activator CBP

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