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http://purl.uniprot.org/citations/12402045http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12402045http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12402045http://www.w3.org/2000/01/rdf-schema#comment"Ubiquitin-mediated proteolysis of securin and mitotic cyclins is essential for exit from mitosis. The final step in ubiquitination of these and other proteins is catalysed by the anaphase-promoting complex (APC), a multi-subunit ubiquitin-protein ligase (E3). Little is known about the molecular reaction resulting in APC-dependent substrate ubiquitination or the role of individual APC subunits in the reaction. Using a well-defined in vitro system, we show that highly purified APC from Saccharomyces cerevisiae ubiquitinates a model cyclin substrate in a processive manner. Analysis of mutant APC lacking the Doc1/Apc10 subunit (APC(doc1 Delta)) indicates that Doc1 is required for processivity. The specific molecular defect in APC(doc1 Delta) is identified by a large increase in apparent K(M) for the cyclin substrate relative to the wild-type enzyme. This suggests that Doc1 stimulates processivity by limiting substrate dissociation. Addition of recombinant Doc1 to APC(doc1 Delta) fully restores enzyme function. Doc1-related domains are found in mechanistically distinct ubiquitin-ligase enzymes and may generally stimulate ubiquitination by contributing to substrate-enzyme affinity."xsd:string
http://purl.uniprot.org/citations/12402045http://purl.org/dc/terms/identifier"doi:10.1038/ncb871"xsd:string
http://purl.uniprot.org/citations/12402045http://purl.org/dc/terms/identifier"doi:10.1038/ncb871"xsd:string
http://purl.uniprot.org/citations/12402045http://purl.uniprot.org/core/author"Morgan D.O."xsd:string
http://purl.uniprot.org/citations/12402045http://purl.uniprot.org/core/author"Morgan D.O."xsd:string
http://purl.uniprot.org/citations/12402045http://purl.uniprot.org/core/author"Carroll C.W."xsd:string
http://purl.uniprot.org/citations/12402045http://purl.uniprot.org/core/author"Carroll C.W."xsd:string
http://purl.uniprot.org/citations/12402045http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12402045http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12402045http://purl.uniprot.org/core/name"Nat. Cell Biol."xsd:string
http://purl.uniprot.org/citations/12402045http://purl.uniprot.org/core/name"Nat. Cell Biol."xsd:string
http://purl.uniprot.org/citations/12402045http://purl.uniprot.org/core/pages"880-887"xsd:string
http://purl.uniprot.org/citations/12402045http://purl.uniprot.org/core/pages"880-887"xsd:string
http://purl.uniprot.org/citations/12402045http://purl.uniprot.org/core/title"The Doc1 subunit is a processivity factor for the anaphase-promoting complex."xsd:string
http://purl.uniprot.org/citations/12402045http://purl.uniprot.org/core/title"The Doc1 subunit is a processivity factor for the anaphase-promoting complex."xsd:string
http://purl.uniprot.org/citations/12402045http://purl.uniprot.org/core/volume"4"xsd:string
http://purl.uniprot.org/citations/12402045http://purl.uniprot.org/core/volume"4"xsd:string
http://purl.uniprot.org/citations/12402045http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12402045
http://purl.uniprot.org/citations/12402045http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12402045
http://purl.uniprot.org/citations/12402045http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12402045
http://purl.uniprot.org/citations/12402045http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12402045
http://purl.uniprot.org/uniprot/P53068http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12402045
http://purl.uniprot.org/uniprot/P53068#attribution-2913960051F704A28107982C2E6AF739http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/12402045