http://purl.uniprot.org/citations/14536085 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/14536085 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/14536085 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
http://purl.uniprot.org/citations/14536085 | http://purl.org/dc/terms/identifier | "doi:10.1016/s1097-2765(03)00288-0"xsd:string |
http://purl.uniprot.org/citations/14536085 | http://purl.org/dc/terms/identifier | "doi:10.1016/s1097-2765(03)00288-0"xsd:string |
http://purl.uniprot.org/citations/14536085 | http://purl.org/dc/terms/identifier | "doi:10.1016/S1097-2765(03)00288-0"xsd:string |
http://purl.uniprot.org/citations/14536085 | http://purl.uniprot.org/core/author | "Marmorstein R."xsd:string |
http://purl.uniprot.org/citations/14536085 | http://purl.uniprot.org/core/author | "Marmorstein R."xsd:string |
http://purl.uniprot.org/citations/14536085 | http://purl.uniprot.org/core/author | "Berger S.L."xsd:string |
http://purl.uniprot.org/citations/14536085 | http://purl.uniprot.org/core/author | "Berger S.L."xsd:string |
http://purl.uniprot.org/citations/14536085 | http://purl.uniprot.org/core/author | "Clements A."xsd:string |
http://purl.uniprot.org/citations/14536085 | http://purl.uniprot.org/core/author | "Clements A."xsd:string |
http://purl.uniprot.org/citations/14536085 | http://purl.uniprot.org/core/author | "Lo W.S."xsd:string |
http://purl.uniprot.org/citations/14536085 | http://purl.uniprot.org/core/author | "Lo W.-S."xsd:string |
http://purl.uniprot.org/citations/14536085 | http://purl.uniprot.org/core/author | "Lo W.-S."xsd:string |
http://purl.uniprot.org/citations/14536085 | http://purl.uniprot.org/core/author | "Pillus L."xsd:string |
http://purl.uniprot.org/citations/14536085 | http://purl.uniprot.org/core/author | "Pillus L."xsd:string |
http://purl.uniprot.org/citations/14536085 | http://purl.uniprot.org/core/author | "Poux A.N."xsd:string |
http://purl.uniprot.org/citations/14536085 | http://purl.uniprot.org/core/author | "Poux A.N."xsd:string |
http://purl.uniprot.org/citations/14536085 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
http://purl.uniprot.org/citations/14536085 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
http://purl.uniprot.org/citations/14536085 | http://purl.uniprot.org/core/name | "Mol. Cell"xsd:string |
http://purl.uniprot.org/citations/14536085 | http://purl.uniprot.org/core/name | "Mol. Cell"xsd:string |
http://purl.uniprot.org/citations/14536085 | http://purl.uniprot.org/core/pages | "461-473"xsd:string |
http://purl.uniprot.org/citations/14536085 | http://purl.uniprot.org/core/pages | "461-473"xsd:string |