RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/16714294http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16714294http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16714294http://www.w3.org/2000/01/rdf-schema#comment"Polycomb group proteins Bmi-1 and Ring1B are core subunits of the PRC1 complex, which plays important roles in the regulation of Hox gene expression, X-chromosome inactivation, tumorigenesis, and stem cell self-renewal. The RING finger protein Ring1B is an E3 ligase that participates in the ubiquitination of lysine 119 of histone H2A, and the binding of Bmi-1 stimulates the E3 ligase activity. We have mapped the regions of Bmi-1 and Ring1B required for efficient ubiquitin transfer and determined a 2.5-A structure of the Bmi-1-Ring1B core domain complex. The structure reveals that Ring1B "hugs" Bmi-1 through extensive RING domain contacts and its N-terminal tail wraps around Bmi-1. The two regions of interaction have a synergistic effect on the E3 ligase activity. Our analyses suggest a model where the Bmi-1-Ring1B complex stabilizes the interaction between the E2 enzyme and the nucleosomal substrate to allow efficient ubiquitin transfer."xsd:string
http://purl.uniprot.org/citations/16714294http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m602461200"xsd:string
http://purl.uniprot.org/citations/16714294http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m602461200"xsd:string
http://purl.uniprot.org/citations/16714294http://purl.uniprot.org/core/author"Li Z."xsd:string
http://purl.uniprot.org/citations/16714294http://purl.uniprot.org/core/author"Li Z."xsd:string
http://purl.uniprot.org/citations/16714294http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/16714294http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/16714294http://purl.uniprot.org/core/author"Wang M."xsd:string
http://purl.uniprot.org/citations/16714294http://purl.uniprot.org/core/author"Wang M."xsd:string
http://purl.uniprot.org/citations/16714294http://purl.uniprot.org/core/author"Cao R."xsd:string
http://purl.uniprot.org/citations/16714294http://purl.uniprot.org/core/author"Cao R."xsd:string
http://purl.uniprot.org/citations/16714294http://purl.uniprot.org/core/author"Xu R.M."xsd:string
http://purl.uniprot.org/citations/16714294http://purl.uniprot.org/core/author"Xu R.M."xsd:string
http://purl.uniprot.org/citations/16714294http://purl.uniprot.org/core/author"Myers M.P."xsd:string
http://purl.uniprot.org/citations/16714294http://purl.uniprot.org/core/author"Myers M.P."xsd:string
http://purl.uniprot.org/citations/16714294http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16714294http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16714294http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/16714294http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/16714294http://purl.uniprot.org/core/pages"20643-20649"xsd:string
http://purl.uniprot.org/citations/16714294http://purl.uniprot.org/core/pages"20643-20649"xsd:string
http://purl.uniprot.org/citations/16714294http://purl.uniprot.org/core/title"Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex."xsd:string
http://purl.uniprot.org/citations/16714294http://purl.uniprot.org/core/title"Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex."xsd:string