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http://purl.uniprot.org/citations/20110345http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20110345http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20110345http://www.w3.org/2000/01/rdf-schema#comment"Rad17 is critical for the ATR-dependent activation of Chk1 during checkpoint responses. It is known that Rad17 loads the Rad9-Hus1-Rad1 (9-1-1) complex onto DNA. We show that Rad17 also mediates the interaction of 9-1-1 with the ATR-activating protein TopBP1 in Xenopus egg extracts. Studies with Rad17 mutants indicate that binding of ATP to Rad17 is essential for the association of 9-1-1 and TopBP1. Furthermore, hydrolysis of ATP by Rad17 is necessary for the loading of 9-1-1 onto DNA and the elevated, checkpoint-dependent accumulation of TopBP1 on chromatin. Significantly, a mutant 9-1-1 complex that cannot bind TopBP1 has a normal capacity to promote elevated accumulation of TopBP1 on chromatin. Taken together, we propose the following mechanism. First, Rad17 loads 9-1-1 onto DNA. Second, TopBP1 accumulates on chromatin in a manner that depends on both Rad17 and 9-1-1. Finally, 9-1-1 and TopBP1 dock in a Rad17-dependent manner before activation of Chk1."xsd:string
http://purl.uniprot.org/citations/20110345http://purl.org/dc/terms/identifier"doi:10.1091/mbc.e09-11-0958"xsd:string
http://purl.uniprot.org/citations/20110345http://purl.uniprot.org/core/author"Dunphy W.G."xsd:string
http://purl.uniprot.org/citations/20110345http://purl.uniprot.org/core/author"Dunphy W.G."xsd:string
http://purl.uniprot.org/citations/20110345http://purl.uniprot.org/core/author"Lee J."xsd:string
http://purl.uniprot.org/citations/20110345http://purl.uniprot.org/core/author"Lee J."xsd:string
http://purl.uniprot.org/citations/20110345http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20110345http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20110345http://purl.uniprot.org/core/name"Mol. Biol. Cell"xsd:string
http://purl.uniprot.org/citations/20110345http://purl.uniprot.org/core/name"Mol Biol Cell"xsd:string
http://purl.uniprot.org/citations/20110345http://purl.uniprot.org/core/pages"926-935"xsd:string
http://purl.uniprot.org/citations/20110345http://purl.uniprot.org/core/pages"926-935"xsd:string
http://purl.uniprot.org/citations/20110345http://purl.uniprot.org/core/title"Rad17 plays a central role in establishment of the interaction between TopBP1 and the Rad9-Hus1-Rad1 complex at stalled replication forks."xsd:string
http://purl.uniprot.org/citations/20110345http://purl.uniprot.org/core/title"Rad17 plays a central role in establishment of the interaction between TopBP1 and the Rad9-Hus1-Rad1 complex at stalled replication forks."xsd:string
http://purl.uniprot.org/citations/20110345http://purl.uniprot.org/core/volume"21"xsd:string
http://purl.uniprot.org/citations/20110345http://purl.uniprot.org/core/volume"21"xsd:string
http://purl.uniprot.org/citations/20110345http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20110345
http://purl.uniprot.org/citations/20110345http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20110345
http://purl.uniprot.org/citations/20110345http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20110345
http://purl.uniprot.org/citations/20110345http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20110345
http://purl.uniprot.org/uniprot/Q8AY27http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/20110345
http://purl.uniprot.org/uniprot/Q7ZZU5http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/20110345
http://purl.uniprot.org/uniprot/Q6INE0http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/20110345