http://purl.uniprot.org/citations/21454705 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/21454705 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/21454705 | http://www.w3.org/2000/01/rdf-schema#comment | "The histone chaperone Vps75 presents the remarkable property of stimulating the Rtt109-dependent acetylation of several histone H3 lysine residues within (H3-H4)(2) tetramers. To investigate this activation mechanism, we determined x-ray structures of full-length Vps75 in complex with full-length Rtt109 in two crystal forms. Both structures show similar asymmetric assemblies of a Vps75 dimer bound to an Rtt109 monomer. In the Vps75-Rtt109 complexes, the catalytic site of Rtt109 is confined to an enclosed space that can accommodate the N-terminal tail of histone H3 in (H3-H4)(2). Investigation of Vps75-Rtt109-(H3-H4)(2) and Vps75-(H3-H4)(2) complexes by NMR spectroscopy-probed hydrogen/deuterium exchange suggests that Vps75 guides histone H3 in the catalytic enclosure. These findings clarify the basis for the enhanced acetylation of histone H3 tail residues by Vps75-Rtt109."xsd:string |
http://purl.uniprot.org/citations/21454705 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.c111.220715"xsd:string |
http://purl.uniprot.org/citations/21454705 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.c111.220715"xsd:string |
http://purl.uniprot.org/citations/21454705 | http://purl.uniprot.org/core/author | "Hu Q."xsd:string |
http://purl.uniprot.org/citations/21454705 | http://purl.uniprot.org/core/author | "Hu Q."xsd:string |
http://purl.uniprot.org/citations/21454705 | http://purl.uniprot.org/core/author | "Zhang Z."xsd:string |
http://purl.uniprot.org/citations/21454705 | http://purl.uniprot.org/core/author | "Zhang Z."xsd:string |
http://purl.uniprot.org/citations/21454705 | http://purl.uniprot.org/core/author | "Zhou H."xsd:string |
http://purl.uniprot.org/citations/21454705 | http://purl.uniprot.org/core/author | "Zhou H."xsd:string |
http://purl.uniprot.org/citations/21454705 | http://purl.uniprot.org/core/author | "Su D."xsd:string |
http://purl.uniprot.org/citations/21454705 | http://purl.uniprot.org/core/author | "Su D."xsd:string |
http://purl.uniprot.org/citations/21454705 | http://purl.uniprot.org/core/author | "Xu R.M."xsd:string |
http://purl.uniprot.org/citations/21454705 | http://purl.uniprot.org/core/author | "Xu R.M."xsd:string |
http://purl.uniprot.org/citations/21454705 | http://purl.uniprot.org/core/author | "Thompson J.R."xsd:string |
http://purl.uniprot.org/citations/21454705 | http://purl.uniprot.org/core/author | "Thompson J.R."xsd:string |
http://purl.uniprot.org/citations/21454705 | http://purl.uniprot.org/core/author | "Mer G."xsd:string |
http://purl.uniprot.org/citations/21454705 | http://purl.uniprot.org/core/author | "Mer G."xsd:string |
http://purl.uniprot.org/citations/21454705 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
http://purl.uniprot.org/citations/21454705 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
http://purl.uniprot.org/citations/21454705 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/21454705 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/21454705 | http://purl.uniprot.org/core/pages | "15625-15629"xsd:string |
http://purl.uniprot.org/citations/21454705 | http://purl.uniprot.org/core/pages | "15625-15629"xsd:string |