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http://purl.uniprot.org/citations/30295604http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30295604http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30295604http://www.w3.org/2000/01/rdf-schema#comment"TOPBP1 and its fission yeast homologueRad4, are critical players in a range of DNA replication, repair and damage signalling processes. They are composed of multiple BRCT domains, some of which bind phosphorylated motifs in other proteins. They thus act as multi-point adaptors bringing proteins together into functional combinations, dependent on post-translational modifications downstream of cell cycle and DNA damage signals. We have now structurally and/or biochemically characterised a sufficient number of high-affinity complexes for the conserved N-terminal region of TOPBP1 and Rad4 with diverse phospho-ligands, including human RAD9 and Treslin, and Schizosaccharomyces pombe Crb2 and Sld3, to define the determinants of BRCT domain specificity. We use this to identify and characterise previously unknown phosphorylation-dependent TOPBP1/Rad4-binding motifs in human RHNO1 and the fission yeast homologue of MDC1, Mdb1. These results provide important insights into how multiple BRCT domains within TOPBP1/Rad4 achieve selective and combinatorial binding of their multiple partner proteins."xsd:string
http://purl.uniprot.org/citations/30295604http://purl.org/dc/terms/identifier"doi:10.7554/elife.39979"xsd:string
http://purl.uniprot.org/citations/30295604http://purl.org/dc/terms/identifier"doi:10.7554/elife.39979"xsd:string
http://purl.uniprot.org/citations/30295604http://purl.uniprot.org/core/author"Oliver A.W."xsd:string
http://purl.uniprot.org/citations/30295604http://purl.uniprot.org/core/author"Oliver A.W."xsd:string
http://purl.uniprot.org/citations/30295604http://purl.uniprot.org/core/author"Pearl L.H."xsd:string
http://purl.uniprot.org/citations/30295604http://purl.uniprot.org/core/author"Pearl L.H."xsd:string
http://purl.uniprot.org/citations/30295604http://purl.uniprot.org/core/author"Rappas M."xsd:string
http://purl.uniprot.org/citations/30295604http://purl.uniprot.org/core/author"Rappas M."xsd:string
http://purl.uniprot.org/citations/30295604http://purl.uniprot.org/core/author"Day M."xsd:string
http://purl.uniprot.org/citations/30295604http://purl.uniprot.org/core/author"Day M."xsd:string
http://purl.uniprot.org/citations/30295604http://purl.uniprot.org/core/author"Boos D."xsd:string
http://purl.uniprot.org/citations/30295604http://purl.uniprot.org/core/author"Boos D."xsd:string
http://purl.uniprot.org/citations/30295604http://purl.uniprot.org/core/author"Ptasinska K."xsd:string
http://purl.uniprot.org/citations/30295604http://purl.uniprot.org/core/author"Ptasinska K."xsd:string
http://purl.uniprot.org/citations/30295604http://purl.uniprot.org/core/date"2018"xsd:gYear
http://purl.uniprot.org/citations/30295604http://purl.uniprot.org/core/date"2018"xsd:gYear
http://purl.uniprot.org/citations/30295604http://purl.uniprot.org/core/name"Elife"xsd:string
http://purl.uniprot.org/citations/30295604http://purl.uniprot.org/core/name"Elife"xsd:string
http://purl.uniprot.org/citations/30295604http://purl.uniprot.org/core/pages"e39979"xsd:string
http://purl.uniprot.org/citations/30295604http://purl.uniprot.org/core/pages"e39979"xsd:string
http://purl.uniprot.org/citations/30295604http://purl.uniprot.org/core/title"BRCT domains of the DNA damage checkpoint proteins TOPBP1/Rad4 display distinct specificities for phosphopeptide ligands. ."xsd:string
http://purl.uniprot.org/citations/30295604http://purl.uniprot.org/core/title"BRCT domains of the DNA damage checkpoint proteins TOPBP1/Rad4 display distinct specificities for phosphopeptide ligands."xsd:string