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

The transcription initiation factor TFIID is a multimeric protein complex composed of TATA box-binding protein (TBP) and many TBP-associated factors (TAF sub(II)s). TAF sub(II)s are important cofactors that mediate activated transcription by providing interaction sites for distinct activators. Here,...

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Bibliographic Details
Published in:Cell 1996-12, Vol.87 (7), p.1261-1270
Main Authors: Mizzen, CA, Yang, Xiang-Jiao, Kokubo, T, Brownell, JE, Bannister, A J, Owen-Hughes, T, Workman, J, Wang, Lian, Berger, S L, Kouzarides, T, Nakatani, Yoshihiro, Allis, C D
Format: Article
Language:English
Subjects:
Drosophila
Saccharomyces cerevisiae
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Summary:The transcription initiation factor TFIID is a multimeric protein complex composed of TATA box-binding protein (TBP) and many TBP-associated factors (TAF sub(II)s). TAF sub(II)s are important cofactors that mediate activated transcription by providing interaction sites for distinct activators. Here, we present evidence that human TAF sub(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 sub(II)230 and yTAF sub(II)130. The HAT activity of dTAF sub(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 sub(II)250 may be involved in mechanisms by which TFIID gains access to transcriptionally repressed chromatin.
ISSN:0092-8674