The TAF(II)250 subunit of TFIID has histone acetyltransferase activity

Craig A. Mizzen; Xiang Jiao Yang; Tetsuro Kokubo; James E. Brownell; Andrew J. Bannister; Tom Owen-Hughes; Jerry Workman; Lian Wang; Shelley L. Berger; Tony Kouzarides; Yoshihiro Nakatani; C. David Allis

doi:10.1016/S0092-8674(00)81821-8

The TAF(II)250 subunit of TFIID has histone acetyltransferase activity

Craig A. Mizzen, Xiang Jiao Yang, Tetsuro Kokubo, James E. Brownell, Andrew J. Bannister, Tom Owen-Hughes, Jerry Workman, Lian Wang, Shelley L. Berger, Tony Kouzarides, Yoshihiro Nakatani, C. David Allis

Research output: Contribution to journal › Article › peer-review

Abstract

The transcription initiation factor TFIID is a multimeric protein complex composed of TATA box-binding protein (TBP) and many TBP-associated factors (TAF(II)s). TAF(II)s are important cofactors that mediate activated transcription by providing interaction sites for distinct activators. Here, we present evidence that human TAF(II)250 and its homologs in Drosophila and yeast have histone acetyltransferase (HAT) activity in vitro. HAT activity maps to the central, most conserved portion of dTAF(II)230 and yTAF(II)130. The HAT activity of dTAF(II)230 resembles that of yeast and human GCN5 in that it is specific for histones H3 and H4 in vitro. Our findings suggest that targeted histone acetylation at specific promoters by TAF(II)250 may be involved in mechanisms by which TFIID gains access to transcriptionally repressed chromatin.

Original language	English (US)
Pages (from-to)	1261-1270
Number of pages	10
Journal	Cell
Volume	87
Issue number	7
DOIs	https://doi.org/10.1016/S0092-8674(00)81821-8
State	Published - Dec 27 1996
Externally published	Yes

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology

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10.1016/S0092-8674(00)81821-8

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title = "The TAF(II)250 subunit of TFIID has histone acetyltransferase activity",

abstract = "The transcription initiation factor TFIID is a multimeric protein complex composed of TATA box-binding protein (TBP) and many TBP-associated factors (TAF(II)s). TAF(II)s are important cofactors that mediate activated transcription by providing interaction sites for distinct activators. Here, we present evidence that human TAF(II)250 and its homologs in Drosophila and yeast have histone acetyltransferase (HAT) activity in vitro. HAT activity maps to the central, most conserved portion of dTAF(II)230 and yTAF(II)130. The HAT activity of dTAF(II)230 resembles that of yeast and human GCN5 in that it is specific for histones H3 and H4 in vitro. Our findings suggest that targeted histone acetylation at specific promoters by TAF(II)250 may be involved in mechanisms by which TFIID gains access to transcriptionally repressed chromatin.",

author = "Mizzen, {Craig A.} and Yang, {Xiang Jiao} and Tetsuro Kokubo and Brownell, {James E.} and Bannister, {Andrew J.} and Tom Owen-Hughes and Jerry Workman and Lian Wang and Berger, {Shelley L.} and Tony Kouzarides and Yoshihiro Nakatani and Allis, {C. David}",

year = "1996",

month = dec,

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doi = "10.1016/S0092-8674(00)81821-8",

language = "English (US)",

volume = "87",

pages = "1261--1270",

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T1 - The TAF(II)250 subunit of TFIID has histone acetyltransferase activity

AU - Mizzen, Craig A.

AU - Yang, Xiang Jiao

AU - Kokubo, Tetsuro

AU - Brownell, James E.

AU - Bannister, Andrew J.

AU - Owen-Hughes, Tom

AU - Workman, Jerry

AU - Wang, Lian

AU - Berger, Shelley L.

AU - Kouzarides, Tony

AU - Nakatani, Yoshihiro

AU - Allis, C. David

PY - 1996/12/27

Y1 - 1996/12/27

N2 - The transcription initiation factor TFIID is a multimeric protein complex composed of TATA box-binding protein (TBP) and many TBP-associated factors (TAF(II)s). TAF(II)s are important cofactors that mediate activated transcription by providing interaction sites for distinct activators. Here, we present evidence that human TAF(II)250 and its homologs in Drosophila and yeast have histone acetyltransferase (HAT) activity in vitro. HAT activity maps to the central, most conserved portion of dTAF(II)230 and yTAF(II)130. The HAT activity of dTAF(II)230 resembles that of yeast and human GCN5 in that it is specific for histones H3 and H4 in vitro. Our findings suggest that targeted histone acetylation at specific promoters by TAF(II)250 may be involved in mechanisms by which TFIID gains access to transcriptionally repressed chromatin.

AB - The transcription initiation factor TFIID is a multimeric protein complex composed of TATA box-binding protein (TBP) and many TBP-associated factors (TAF(II)s). TAF(II)s are important cofactors that mediate activated transcription by providing interaction sites for distinct activators. Here, we present evidence that human TAF(II)250 and its homologs in Drosophila and yeast have histone acetyltransferase (HAT) activity in vitro. HAT activity maps to the central, most conserved portion of dTAF(II)230 and yTAF(II)130. The HAT activity of dTAF(II)230 resembles that of yeast and human GCN5 in that it is specific for histones H3 and H4 in vitro. Our findings suggest that targeted histone acetylation at specific promoters by TAF(II)250 may be involved in mechanisms by which TFIID gains access to transcriptionally repressed chromatin.

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DO - 10.1016/S0092-8674(00)81821-8

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JO - Cell

JF - Cell

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ER -

The TAF(II)250 subunit of TFIID has histone acetyltransferase activity

Abstract

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