pubmed-article:8601308 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8601308 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
pubmed-article:8601308 | lifeskim:mentions | umls-concept:C0062773 | lld:lifeskim |
pubmed-article:8601308 | lifeskim:mentions | umls-concept:C1156200 | lld:lifeskim |
pubmed-article:8601308 | lifeskim:mentions | umls-concept:C0017255 | lld:lifeskim |
pubmed-article:8601308 | lifeskim:mentions | umls-concept:C0039679 | lld:lifeskim |
pubmed-article:8601308 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
pubmed-article:8601308 | lifeskim:mentions | umls-concept:C1171569 | lld:lifeskim |
pubmed-article:8601308 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:8601308 | pubmed:dateCreated | 1996-5-9 | lld:pubmed |
pubmed-article:8601308 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8601308 | pubmed:abstractText | We 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:8601308 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8601308 | pubmed:language | eng | lld:pubmed |
pubmed-article:8601308 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8601308 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8601308 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:8601308 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8601308 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8601308 | pubmed:month | Mar | lld:pubmed |
pubmed-article:8601308 | pubmed:issn | 0092-8674 | lld:pubmed |
pubmed-article:8601308 | pubmed:author | pubmed-author:KobayashiRR | lld:pubmed |
pubmed-article:8601308 | pubmed:author | pubmed-author:AllisC DCD | lld:pubmed |
pubmed-article:8601308 | pubmed:author | pubmed-author:ZhouJJ | lld:pubmed |
pubmed-article:8601308 | pubmed:author | pubmed-author:EdmondsonD... | lld:pubmed |
pubmed-article:8601308 | pubmed:author | pubmed-author:RothS YSY | lld:pubmed |
pubmed-article:8601308 | pubmed:author | pubmed-author:BrownellJ EJE | lld:pubmed |
pubmed-article:8601308 | pubmed:author | pubmed-author:RanalliTT | lld:pubmed |
pubmed-article:8601308 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8601308 | pubmed:day | 22 | lld:pubmed |
pubmed-article:8601308 | pubmed:volume | 84 | lld:pubmed |
pubmed-article:8601308 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8601308 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8601308 | pubmed:pagination | 843-51 | lld:pubmed |
pubmed-article:8601308 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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pubmed-article:8601308 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8601308 | pubmed:articleTitle | Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation. | lld:pubmed |
pubmed-article:8601308 | pubmed:affiliation | Department of Biology, University of Rochester, New York, 14627, USA. | lld:pubmed |
pubmed-article:8601308 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8601308 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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