| pubmed-article:8980232 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8980232 | lifeskim:mentions | umls-concept:C1146629 | lld:lifeskim |
| pubmed-article:8980232 | lifeskim:mentions | umls-concept:C0076919 | lld:lifeskim |
| pubmed-article:8980232 | lifeskim:mentions | umls-concept:C1151928 | lld:lifeskim |
| pubmed-article:8980232 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:8980232 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:8980232 | pubmed:dateCreated | 1997-2-3 | lld:pubmed |
| pubmed-article:8980232 | pubmed:abstractText | 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. | lld:pubmed |
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| pubmed-article:8980232 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8980232 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8980232 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8980232 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:8980232 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:8980232 | pubmed:author | pubmed-author:WangLL | lld:pubmed |
| pubmed-article:8980232 | pubmed:author | pubmed-author:AllisC DCD | lld:pubmed |
| pubmed-article:8980232 | pubmed:author | pubmed-author:KokuboTT | lld:pubmed |
| pubmed-article:8980232 | pubmed:author | pubmed-author:NakataniYY | lld:pubmed |
| pubmed-article:8980232 | pubmed:author | pubmed-author:BergerS LSL | lld:pubmed |
| pubmed-article:8980232 | pubmed:author | pubmed-author:KouzaridesTT | lld:pubmed |
| pubmed-article:8980232 | pubmed:author | pubmed-author:BannisterA... | lld:pubmed |
| pubmed-article:8980232 | pubmed:author | pubmed-author:MizzenC ACA | lld:pubmed |
| pubmed-article:8980232 | pubmed:author | pubmed-author:YangX JXJ | lld:pubmed |
| pubmed-article:8980232 | pubmed:author | pubmed-author:WorkmanJJ | lld:pubmed |
| pubmed-article:8980232 | pubmed:author | pubmed-author:Owen-HughesTT | lld:pubmed |
| pubmed-article:8980232 | pubmed:author | pubmed-author:BrownellJ EJE | lld:pubmed |
| pubmed-article:8980232 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8980232 | pubmed:day | 27 | lld:pubmed |
| pubmed-article:8980232 | pubmed:volume | 87 | lld:pubmed |
| pubmed-article:8980232 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8980232 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8980232 | pubmed:pagination | 1261-70 | lld:pubmed |
| pubmed-article:8980232 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:8980232 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8980232 | pubmed:articleTitle | The TAF(II)250 subunit of TFIID has histone acetyltransferase activity. | lld:pubmed |
| pubmed-article:8980232 | pubmed:affiliation | Department of Biology, University of Rochester, New York 14627, USA. | lld:pubmed |
| pubmed-article:8980232 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8980232 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8980232 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:8980232 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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