HIV-1 Tat binds TAF<sub>II</sub>250 and represses TAF<sub>II</sub>250-dependent transcription of major histocompatibility class I genes

Weissman, Jocelyn D.; Brown, Julie; Howcroft, T. Kevin; Hwang, Jae Ryoung; Chawla, Ashish; Roche, Paul A.; Schiltz, Louis; Nakatani, Y.; Singer, Dinah S.

doi:10.1073/pnas.95.20.11601

Cited by 135 publications

(128 citation statements)

References 43 publications

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“…Repression results from the interaction of Tat with TAFII250 (a unique HAT), the largest subunit of TFIID. The C terminal domain of Tat interacts with the HAT domain of TAFII250 and inhibits its HAT activity (37). Interestingly the promoters that are repressed by Tat require the presence of TAFII250.…”

Section: Classification Of Nonhistone Substrates Of Hats and Hdacsmentioning

confidence: 99%

“…HAT enzymes are important for HIV replication. Treatment of latent HIV containing cells with HDAC inhibitors breaks the HIV latency, presumably by enhancement of acetylation of transactivator Tat and the nucleosomes in LTR (37). Abnormality caused by the improper acetylation status of nonhistone proteins per se, has not been studied systematically.…”

Section: Alteration Of Acetylation Status Of Nonhistone Proteins and mentioning

confidence: 99%

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Transcriptional Regulation by the Acetylation of Nonhistone Proteins in Humans – A New Target for Therapeutics

Das

Kundu

2005

IUBMB Life (International Union of Biochemistry and Molecular B

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SummaryGene expression from the dynamic chromatin template is regulated by certain key cellular players that cause post-translational modifications of both histones and nonhistone proteins. The acetyltransferases and deacetylases are two such key groups of enzymes that play crucial roles in maintaining the reversible acetylation status of histones and nonhistone proteins. Emerging evidence suggests that acetylation of nonhistone protein is equally important in the transcription regulation as the histone acetylation. Since dysfunction of HATs and HDACs leads to several diseases, aberrant acetylation of nonhistone protein is also associated with diseases. Small molecule modulators of these enzymes, which may help in maintaining the normal cellular acetylation status of these proteins, have important therapeutic implications. IUBMB Life, 57: 137 -148, 2005

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Section: Classification Of Nonhistone Substrates Of Hats and Hdacsmentioning

confidence: 99%

Section: Alteration Of Acetylation Status Of Nonhistone Proteins and mentioning

confidence: 99%

Transcriptional Regulation by the Acetylation of Nonhistone Proteins in Humans – A New Target for Therapeutics

Das

Kundu

2005

IUBMB Life (International Union of Biochemistry and Molecular B

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“…Thus, in ts13 cells with a temperature-sensitive mutation in TAF1, MHC class I expression is abrogated at the nonpermissive temperature. Similarly, MHC class I transcription is inhibited, both in vitro and in vivo, by the transactivator, HIV Tat, which binds to the TAF1 AT domain and inhibits its enzymatic activity (35). Of particular interest, we recently reported that TAF7, a TFIID component, also binds to TAF1 and inhibits its AT activity, resulting in repression of MHC class I transcription (36).…”

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confidence: 99%

TAF7: A possible transcription initiation check-point regulator

Gégonne

Weissman

Zhou

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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Transcription consists of a series of highly regulated steps: assembly of a preinitiation complex (PIC) at the promoter nucleated by TFIID, followed by initiation, elongation, and termination. The present study has focused on the role of the TFIID component, TAF7, in regulating transcription initiation. In TFIID, TAF7 binds to TAF1 and inhibits its intrinsic acetyl transferase activity. We now report that although TAF7 remains bound to TAF1 and associated with TFIID during the formation of the PIC, TAF7 dissociates from the PIC upon transcription initiation. Entry of polymerase II into the assembling PIC is associated with TAF1 and TAF7 phosphorylation, coincident with TAF7 release. We propose that the TFIID composition is dynamic and that TAF7 functions as a check-point regulator suppressing premature transcription initiation until PIC assembly is complete.MHC class I ͉ regulation ͉ preinitiation complex ͉ TFIID I n eukaryotic cells, expression of most protein-encoding genes depends on the RNA polymerase II (Pol II)-dependent transcription machinery. The RNA Pol II machinery assembled on the promoter is composed of distinct complexes that are responsible for effecting the sequential steps of transcription initiation and elongation (1-5). The first step in transcription is the recognition of the core promoter by the TFIID complex and the assembly of a preinitiation complex (PIC) through an ordered recruitment of the general transcription factors (GTFs) TFIIB and TFIIA, followed by the RNA Pol II holoenzyme, the mediator and the remaining GTFs, TFIIF, TFIIE, and TFIIH. Once the PIC has been assembled, transcription initiation ensues: local melting of the promoter DNA, formation of the first phosphodiester bond, followed by the synthesis of a short nascent RNA at which point the polymerase pauses. The initiation of transcription is accompanied by the phosphorylation of serine 5 in the C-terminal domain (CTD) heptad repeat of RNA Pol II (CTD) by the kinase subunit of TFIIH, CDK7 (6-9).Despite the extensive understanding of the general requirements of transcription, many details remain unresolved and there is considerable variation among different promoters and cell types. Promoter recognition is mediated by members of either the TFIID complex family (TFIID, TFIID-like) or the SAGA complex family (e.g., TFTC, PCAF, SAGA) (10-12). In yeast, 90% of gene expression is TFIID-dependent transcription; the remaining 10% is largely dependent on the SAGA complex (13). The TFIID complexes are composed of either the TATAbinding protein (TBP) or a TBP related protein (TRF1, TRF2) and several TBP-associated factors (TAFs) (14-17). The SAGA family complexes do not contain TBP or TBP-related proteins; rather, they contain a GCN5-related histone acetyl transferase (AT) subunit, several adapter and Spt proteins and a subset of TAFs. The composition of the TAFs present in these different complexes varies depending on the structure of the promoter and the cell cycle and tissue-specific gene expression requirement. For example, in yeas...

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“…Apoptosis contributes to the massive depletion of CD4 ϩ T-cells and consequently to the loss of immune competence during HIV-1 infection (43,44). Other effects of extracellular Tat include inhibition of the proliferation of uninfected T-cells (24,37,45), possibly by repression of major histocompatibility complex class I transcription (46); regulation of the expression of the HIV-1 coreceptor CXC chemokine receptor-4 on T-lymphocytes (47); and repression of the expression of manganese-superoxide dismutase (48).…”

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confidence: 99%

The Glutamine-rich Region of the HIV-1 Tat Protein Is Involved in T-cell Apoptosis

Campbell

Pasquier

Watkins

et al. 2004

Journal of Biological Chemistry

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HIV-1 Tat binds TAF_II250 and represses TAF_II250-dependent transcription of major histocompatibility class I genes

Abstract: HIV Tat

Cited by 135 publications

References 43 publications

Transcriptional Regulation by the Acetylation of Nonhistone Proteins in Humans – A New Target for Therapeutics

Transcriptional Regulation by the Acetylation of Nonhistone Proteins in Humans – A New Target for Therapeutics

TAF7: A possible transcription initiation check-point regulator

The Glutamine-rich Region of the HIV-1 Tat Protein Is Involved in T-cell Apoptosis

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HIV-1 Tat binds TAFII250 and represses TAFII250-dependent transcription of major histocompatibility class I genes

Abstract: HIV Tat

Cited by 135 publications

References 43 publications

Transcriptional Regulation by the Acetylation of Nonhistone Proteins in Humans – A New Target for Therapeutics

Transcriptional Regulation by the Acetylation of Nonhistone Proteins in Humans – A New Target for Therapeutics

TAF7: A possible transcription initiation check-point regulator

The Glutamine-rich Region of the HIV-1 Tat Protein Is Involved in T-cell Apoptosis

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HIV-1 Tat binds TAF_II250 and represses TAF_II250-dependent transcription of major histocompatibility class I genes