| pubmed-article:17179179 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17179179 | lifeskim:mentions | umls-concept:C0019652 | lld:lifeskim |
| pubmed-article:17179179 | lifeskim:mentions | umls-concept:C0040649 | lld:lifeskim |
| pubmed-article:17179179 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
| pubmed-article:17179179 | lifeskim:mentions | umls-concept:C2752385 | lld:lifeskim |
| pubmed-article:17179179 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:17179179 | pubmed:dateCreated | 2007-2-19 | lld:pubmed |
| pubmed-article:17179179 | pubmed:abstractText | Histone chaperones are thought to be important for maintaining the physiological activity of histones; however, their exact roles are not fully understood. The physiological function of template activating factor (TAF)-I, one of the histone chaperones, also remains unclear; however, its biochemical properties have been well studied. By performing microarray analyses, we found that TAF-I stimulates the transcription of a sub-set of genes. The transcription of endogenous genes that was up-regulated by TAF-I was found to be additively stimulated by histone acetylation. On performing an experiment with a cell line containing a model gene integrated into the chromosome, TAF-I was found to stimulate the model gene transcription in a histone chaperone activity-dependent manner additively with histone acetylation. TAF-I bound to the core histones and remodeled the chromatin structure independent of the N-terminal histone tail and its acetylation level in vitro. These results suggest that TAF-I remodel the chromatin structure through its interaction with the core domain of the histones, including the histone fold, and this mechanism is independent of the histone acetylation status. | lld:pubmed |
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| pubmed-article:17179179 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:17179179 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17179179 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17179179 | pubmed:issn | 1362-4962 | lld:pubmed |
| pubmed-article:17179179 | pubmed:author | pubmed-author:NagataKyosuke... | lld:pubmed |
| pubmed-article:17179179 | pubmed:author | pubmed-author:OkuwakiMitsur... | lld:pubmed |
| pubmed-article:17179179 | pubmed:author | pubmed-author:Miyaji-Yamagu... | lld:pubmed |
| pubmed-article:17179179 | pubmed:author | pubmed-author:KatoKohsukeK | lld:pubmed |
| pubmed-article:17179179 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:17179179 | pubmed:volume | 35 | lld:pubmed |
| pubmed-article:17179179 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17179179 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17179179 | pubmed:pagination | 705-15 | lld:pubmed |
| pubmed-article:17179179 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:17179179 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17179179 | pubmed:articleTitle | Histone acetylation-independent transcription stimulation by a histone chaperone. | lld:pubmed |
| pubmed-article:17179179 | pubmed:affiliation | Department of Infection Biology, Graduate School of Comprehensive Human Sciences and Institute of Basic Medical Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba 305-8575, Japan. | lld:pubmed |
| pubmed-article:17179179 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17179179 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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