| pubmed-article:14536085 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14536085 | lifeskim:mentions | umls-concept:C0019652 | lld:lifeskim |
| pubmed-article:14536085 | lifeskim:mentions | umls-concept:C0062773 | lld:lifeskim |
| pubmed-article:14536085 | lifeskim:mentions | umls-concept:C1415020 | lld:lifeskim |
| pubmed-article:14536085 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:14536085 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:14536085 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:14536085 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:14536085 | pubmed:dateCreated | 2003-10-10 | lld:pubmed |
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| pubmed-article:14536085 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14536085 | pubmed:abstractText | Distinct posttranslational modifications on histones occur in specific patterns to mediate certain chromosomal events. For example, on histone H3, phosphorylation at Ser10 can enhance GCN5-mediated Lys14 acetylation to promote transcription. To gain insight into the mechanism underlying this synergism, we determined the structure of Tetrahymena GCN5 (tGCN5) and coenzyme A (CoA) bound to unmodified and Ser10-phosphorylated 19 residue histone H3 peptides (H3p19 and H3p19Pi, respectively). The tGCN5/CoA/H3p19 structure reveals that a 12 amino acid core sequence mediates extensive contacts with the protein, providing the structural basis for substrate specificity by the GCN5/PCAF family of histone acetyltransferases. Comparison with the tGCN5/CoA/H3p19Pi structure reveals that phospho-Ser10 and Thr11 mediate significant histone-protein interactions, and nucleate additional interactions distal to the phosphorylation site. Functional studies show that histone H3 Thr11 is necessary for optimal transcription at yGcn5-dependent promoters requiring Ser10 phosphorylation. Together, these studies reveal how one histone modification can modulate another to affect distinct transcriptional signals. | lld:pubmed |
| pubmed-article:14536085 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14536085 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14536085 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14536085 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:14536085 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14536085 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:14536085 | pubmed:issn | 1097-2765 | lld:pubmed |
| pubmed-article:14536085 | pubmed:author | pubmed-author:BergerShelley... | lld:pubmed |
| pubmed-article:14536085 | pubmed:author | pubmed-author:MarmorsteinRo... | lld:pubmed |
| pubmed-article:14536085 | pubmed:author | pubmed-author:PouxArienne... | lld:pubmed |
| pubmed-article:14536085 | pubmed:author | pubmed-author:PillusLorrain... | lld:pubmed |
| pubmed-article:14536085 | pubmed:author | pubmed-author:ClementsAdrie... | lld:pubmed |
| pubmed-article:14536085 | pubmed:author | pubmed-author:LoWan-ShengWS | lld:pubmed |
| pubmed-article:14536085 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14536085 | pubmed:volume | 12 | lld:pubmed |
| pubmed-article:14536085 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14536085 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14536085 | pubmed:pagination | 461-73 | lld:pubmed |
| pubmed-article:14536085 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:14536085 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:14536085 | pubmed:articleTitle | Structural basis for histone and phosphohistone binding by the GCN5 histone acetyltransferase. | lld:pubmed |
| pubmed-article:14536085 | pubmed:affiliation | The Wistar Institute, Philadelphia, PA 19104, USA. | lld:pubmed |
| pubmed-article:14536085 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14536085 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:14536085 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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