pubmed-article:9674426 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9674426 | lifeskim:mentions | umls-concept:C1336572 | lld:lifeskim |
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pubmed-article:9674426 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
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pubmed-article:9674426 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
pubmed-article:9674426 | lifeskim:mentions | umls-concept:C0449432 | lld:lifeskim |
pubmed-article:9674426 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:9674426 | pubmed:dateCreated | 1998-8-11 | lld:pubmed |
pubmed-article:9674426 | pubmed:abstractText | A number of transcriptional coactivator proteins have been identified as histone acetyltransferase (HAT) proteins, providing a direct molecular basis for the coupling of histone acetylation and transcriptional activation. The yeast Spt-Ada-Gcn5-acetyltransferase (SAGA) complex requires the coactivator protein Gcn5 for HAT activity. Identification of protein subunits by mass spectrometry and immunoblotting revealed that the TATA binding protein-associated factors (TAF(II)s) TAF(II)90, -68/61, -60, -25/23, and -20/17 are integral components of this complex. In addition, TAF(II)68 was required for both SAGA-dependent nucleosomal HAT activity and transcriptional activation from chromatin templates in vitro. These results illustrate a role for certain TAF(II) proteins in the regulation of gene expression at the level of chromatin modification that is distinct from the TFIID complex and TAF(II)145. | lld:pubmed |
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pubmed-article:9674426 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9674426 | pubmed:language | eng | lld:pubmed |
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pubmed-article:9674426 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:9674426 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9674426 | pubmed:month | Jul | lld:pubmed |
pubmed-article:9674426 | pubmed:issn | 0092-8674 | lld:pubmed |
pubmed-article:9674426 | pubmed:author | pubmed-author:GrantP APA | lld:pubmed |
pubmed-article:9674426 | pubmed:author | pubmed-author:YatesJ RJR3rd | lld:pubmed |
pubmed-article:9674426 | pubmed:author | pubmed-author:WorkmanJ LJL | lld:pubmed |
pubmed-article:9674426 | pubmed:author | pubmed-author:ReeseJ CJC | lld:pubmed |
pubmed-article:9674426 | pubmed:author | pubmed-author:StegerD JDJ | lld:pubmed |
pubmed-article:9674426 | pubmed:author | pubmed-author:SchieltzDD | lld:pubmed |
pubmed-article:9674426 | pubmed:author | pubmed-author:Pray-GrantM... | lld:pubmed |
pubmed-article:9674426 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9674426 | pubmed:day | 10 | lld:pubmed |
pubmed-article:9674426 | pubmed:volume | 94 | lld:pubmed |
pubmed-article:9674426 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9674426 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9674426 | pubmed:pagination | 45-53 | lld:pubmed |
pubmed-article:9674426 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:9674426 | pubmed:year | 1998 | lld:pubmed |
pubmed-article:9674426 | pubmed:articleTitle | A subset of TAF(II)s are integral components of the SAGA complex required for nucleosome acetylation and transcriptional stimulation. | lld:pubmed |
pubmed-article:9674426 | pubmed:affiliation | Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park 16802-4500, USA. | lld:pubmed |
pubmed-article:9674426 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9674426 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:9674426 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:9674426 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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