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http://purl.uniprot.org/citations/24507717http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24507717http://www.w3.org/2000/01/rdf-schema#comment"Histone variant H2A.Z-containing nucleosomes exist at most eukaryotic promoters and play important roles in gene transcription and genome stability. The multisubunit nucleosome-remodeling enzyme complex SWR1, conserved from yeast to mammals, catalyzes the ATP-dependent replacement of histone H2A in canonical nucleosomes with H2A.Z. How SWR1 catalyzes the replacement reaction is largely unknown. Here, we determined the crystal structure of the N-terminal region (599-627) of the catalytic subunit Swr1, termed Swr1-Z domain, in complex with the H2A.Z-H2B dimer at 1.78 Å resolution. The Swr1-Z domain forms a 310 helix and an irregular chain. A conserved LxxLF motif in the Swr1-Z 310 helix specifically recognizes the αC helix of H2A.Z. Our results show that the Swr1-Z domain can deliver the H2A.Z-H2B dimer to the DNA-(H3-H4)2 tetrasome to form the nucleosome by a histone chaperone mechanism."xsd:string
http://purl.uniprot.org/citations/24507717http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2014.01.010"xsd:string
http://purl.uniprot.org/citations/24507717http://purl.uniprot.org/core/author"Chen J."xsd:string
http://purl.uniprot.org/citations/24507717http://purl.uniprot.org/core/author"Bai Y."xsd:string
http://purl.uniprot.org/citations/24507717http://purl.uniprot.org/core/author"Feng H."xsd:string
http://purl.uniprot.org/citations/24507717http://purl.uniprot.org/core/author"Jiang J."xsd:string
http://purl.uniprot.org/citations/24507717http://purl.uniprot.org/core/author"Ghirlando R."xsd:string
http://purl.uniprot.org/citations/24507717http://purl.uniprot.org/core/author"Hong J."xsd:string
http://purl.uniprot.org/citations/24507717http://purl.uniprot.org/core/author"Wang F."xsd:string
http://purl.uniprot.org/citations/24507717http://purl.uniprot.org/core/author"Wu C."xsd:string
http://purl.uniprot.org/citations/24507717http://purl.uniprot.org/core/author"Ranjan A."xsd:string
http://purl.uniprot.org/citations/24507717http://purl.uniprot.org/core/author"Xiao T.S."xsd:string
http://purl.uniprot.org/citations/24507717http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24507717http://purl.uniprot.org/core/name"Mol Cell"xsd:string
http://purl.uniprot.org/citations/24507717http://purl.uniprot.org/core/pages"498-505"xsd:string
http://purl.uniprot.org/citations/24507717http://purl.uniprot.org/core/title"The catalytic subunit of the SWR1 remodeler is a histone chaperone for the H2A.Z-H2B dimer."xsd:string
http://purl.uniprot.org/citations/24507717http://purl.uniprot.org/core/volume"53"xsd:string
http://purl.uniprot.org/citations/24507717http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24507717
http://purl.uniprot.org/citations/24507717http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/24507717
http://purl.uniprot.org/uniprot/Q05471#attribution-252BF93A495C556710DE741378541841http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/24507717
http://purl.uniprot.org/uniprot/#_A0A8H8UNN3-mappedCitation-24507717http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24507717
http://purl.uniprot.org/uniprot/#_P02293-mappedCitation-24507717http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24507717
http://purl.uniprot.org/uniprot/#_Q05471-mappedCitation-24507717http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24507717
http://purl.uniprot.org/uniprot/#_Q12692-mappedCitation-24507717http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24507717