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pubmed-article:8601308pubmed:abstractTextWe report the cloning of a transcription-associated histone acetyltransferase type A(HAT A). This Tetrahymena enzyme is strikingly homologous to the yeast protein Gcn5, a putative transcriptional adaptor, and we demonstrate that recombinant Gcn5p possesses HAT activity. Both the ciliate enzyme and Gcn5p contain potential active site residues found in other acetyltransferases and a highly conserved bromodomain. The presence of this domain in nuclear A-type HATs, but not in cytoplasmic B-type HATs, suggests a mechanism whereby HAT A is directed to chromatin to facilitate transcriptional activation. These findings shed light on the biochemical function of the evolutionarily conserved Gcn5p-Ada complex, directly linking histone acetylation to gene activation, and indicate that histone acetylation is a targeted phenomenon.lld:pubmed
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pubmed-article:8601308pubmed:dateRevised2008-11-21lld:pubmed
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pubmed-article:8601308pubmed:articleTitleTetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation.lld:pubmed
pubmed-article:8601308pubmed:affiliationDepartment of Biology, University of Rochester, New York, 14627, USA.lld:pubmed
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pubmed-article:8601308pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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