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http://purl.uniprot.org/citations/20739937http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20739937http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20739937http://www.w3.org/2000/01/rdf-schema#comment"Centromeres are specified epigenetically, and the histone H3 variant CENP-A is assembled into the chromatin of all active centromeres. Divergence from H3 raises the possibility that CENP-A generates unique chromatin features to mark physically centromere location. Here we report the crystal structure of a subnucleosomal heterotetramer, human (CENP-A-H4)(2), that reveals three distinguishing properties encoded by the residues that comprise the CENP-A targeting domain (CATD; ref. 2): (1) a CENP-A-CENP-A interface that is substantially rotated relative to the H3-H3 interface; (2) a protruding loop L1 of the opposite charge as that on H3; and (3) strong hydrophobic contacts that rigidify the CENP-A-H4 interface. Residues involved in the CENP-A-CENP-A rotation are required for efficient incorporation into centromeric chromatin, indicating specificity for an unconventional nucleosome shape. DNA topological analysis indicates that CENP-A-containing nucleosomes are octameric with conventional left-handed DNA wrapping, in contrast to other recent proposals. Our results indicate that CENP-A marks centromere location by restructuring the nucleosome from within its folded histone core."xsd:string
http://purl.uniprot.org/citations/20739937http://purl.org/dc/terms/identifier"doi:10.1038/nature09323"xsd:string
http://purl.uniprot.org/citations/20739937http://purl.org/dc/terms/identifier"doi:10.1038/nature09323"xsd:string
http://purl.uniprot.org/citations/20739937http://purl.uniprot.org/core/author"Black B.E."xsd:string
http://purl.uniprot.org/citations/20739937http://purl.uniprot.org/core/author"Black B.E."xsd:string
http://purl.uniprot.org/citations/20739937http://purl.uniprot.org/core/author"Sekulic N."xsd:string
http://purl.uniprot.org/citations/20739937http://purl.uniprot.org/core/author"Sekulic N."xsd:string
http://purl.uniprot.org/citations/20739937http://purl.uniprot.org/core/author"Bassett E.A."xsd:string
http://purl.uniprot.org/citations/20739937http://purl.uniprot.org/core/author"Bassett E.A."xsd:string
http://purl.uniprot.org/citations/20739937http://purl.uniprot.org/core/author"Rogers D.J."xsd:string
http://purl.uniprot.org/citations/20739937http://purl.uniprot.org/core/author"Rogers D.J."xsd:string
http://purl.uniprot.org/citations/20739937http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20739937http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20739937http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/20739937http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/20739937http://purl.uniprot.org/core/pages"347-351"xsd:string
http://purl.uniprot.org/citations/20739937http://purl.uniprot.org/core/pages"347-351"xsd:string
http://purl.uniprot.org/citations/20739937http://purl.uniprot.org/core/title"The structure of (CENP-A-H4)(2) reveals physical features that mark centromeres."xsd:string
http://purl.uniprot.org/citations/20739937http://purl.uniprot.org/core/title"The structure of (CENP-A-H4)(2) reveals physical features that mark centromeres."xsd:string
http://purl.uniprot.org/citations/20739937http://purl.uniprot.org/core/volume"467"xsd:string
http://purl.uniprot.org/citations/20739937http://purl.uniprot.org/core/volume"467"xsd:string
http://purl.uniprot.org/citations/20739937http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20739937
http://purl.uniprot.org/citations/20739937http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20739937