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http://purl.uniprot.org/citations/21454705http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21454705http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21454705http://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/21454705http://purl.org/dc/terms/identifier"doi:10.1074/jbc.c111.220715"xsd:string
http://purl.uniprot.org/citations/21454705http://purl.org/dc/terms/identifier"doi:10.1074/jbc.c111.220715"xsd:string
http://purl.uniprot.org/citations/21454705http://purl.uniprot.org/core/author"Hu Q."xsd:string
http://purl.uniprot.org/citations/21454705http://purl.uniprot.org/core/author"Hu Q."xsd:string
http://purl.uniprot.org/citations/21454705http://purl.uniprot.org/core/author"Zhang Z."xsd:string
http://purl.uniprot.org/citations/21454705http://purl.uniprot.org/core/author"Zhang Z."xsd:string
http://purl.uniprot.org/citations/21454705http://purl.uniprot.org/core/author"Zhou H."xsd:string
http://purl.uniprot.org/citations/21454705http://purl.uniprot.org/core/author"Zhou H."xsd:string
http://purl.uniprot.org/citations/21454705http://purl.uniprot.org/core/author"Su D."xsd:string
http://purl.uniprot.org/citations/21454705http://purl.uniprot.org/core/author"Su D."xsd:string
http://purl.uniprot.org/citations/21454705http://purl.uniprot.org/core/author"Xu R.M."xsd:string
http://purl.uniprot.org/citations/21454705http://purl.uniprot.org/core/author"Xu R.M."xsd:string
http://purl.uniprot.org/citations/21454705http://purl.uniprot.org/core/author"Thompson J.R."xsd:string
http://purl.uniprot.org/citations/21454705http://purl.uniprot.org/core/author"Thompson J.R."xsd:string
http://purl.uniprot.org/citations/21454705http://purl.uniprot.org/core/author"Mer G."xsd:string
http://purl.uniprot.org/citations/21454705http://purl.uniprot.org/core/author"Mer G."xsd:string
http://purl.uniprot.org/citations/21454705http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21454705http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21454705http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/21454705http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/21454705http://purl.uniprot.org/core/pages"15625-15629"xsd:string
http://purl.uniprot.org/citations/21454705http://purl.uniprot.org/core/pages"15625-15629"xsd:string