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http://purl.uniprot.org/citations/18842000http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18842000http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18842000http://www.w3.org/2000/01/rdf-schema#comment"The BARD1 N-terminal RING domain binds BRCA1 while the BARD1 C-terminal ankyrin and tandem BRCT repeat domains bind CstF-50 to modulate mRNA processing and RNAP II stability in response to DNA damage. Here we characterize the BARD1 structural biochemistry responsible for CstF-50 binding. The crystal structure of the BARD1 BRCT domain uncovers a degenerate phosphopeptide binding pocket lacking the key arginine required for phosphopeptide interactions in other BRCT proteins. Small angle X-ray scattering together with limited proteolysis results indicates that ankyrin and BRCT domains are linked by a flexible tether and do not adopt a fixed orientation relative to one another. Protein pull-down experiments utilizing a series of purified BARD1 deletion mutants indicate that interactions between the CstF-50 WD-40 domain and BARD1 involve the ankyrin-BRCT linker but do not require ankyrin or BRCT domains. The structural plasticity imparted by the ANK-BRCT linker helps to explain the regulated assembly of different protein BARD1 complexes with distinct functions in DNA damage signaling including BARD1-dependent induction of apoptosis plus p53 stabilization and interactions. BARD1 architecture and plasticity imparted by the ANK-BRCT linker are suitable to allow the BARD1 C-terminus to act as a hub with multiple binding sites to integrate diverse DNA damage signals directly to RNA polymerase."xsd:string
http://purl.uniprot.org/citations/18842000http://purl.org/dc/terms/identifier"doi:10.1021/bi801115g"xsd:string
http://purl.uniprot.org/citations/18842000http://purl.org/dc/terms/identifier"doi:10.1021/bi801115g"xsd:string
http://purl.uniprot.org/citations/18842000http://purl.uniprot.org/core/author"Lee M.S."xsd:string
http://purl.uniprot.org/citations/18842000http://purl.uniprot.org/core/author"Lee M.S."xsd:string
http://purl.uniprot.org/citations/18842000http://purl.uniprot.org/core/author"Tainer J.A."xsd:string
http://purl.uniprot.org/citations/18842000http://purl.uniprot.org/core/author"Tainer J.A."xsd:string
http://purl.uniprot.org/citations/18842000http://purl.uniprot.org/core/author"Tsutakawa S.E."xsd:string
http://purl.uniprot.org/citations/18842000http://purl.uniprot.org/core/author"Tsutakawa S.E."xsd:string
http://purl.uniprot.org/citations/18842000http://purl.uniprot.org/core/author"Williams R.S."xsd:string
http://purl.uniprot.org/citations/18842000http://purl.uniprot.org/core/author"Williams R.S."xsd:string
http://purl.uniprot.org/citations/18842000http://purl.uniprot.org/core/author"Edwards R.A."xsd:string
http://purl.uniprot.org/citations/18842000http://purl.uniprot.org/core/author"Edwards R.A."xsd:string
http://purl.uniprot.org/citations/18842000http://purl.uniprot.org/core/author"Glover J.N."xsd:string
http://purl.uniprot.org/citations/18842000http://purl.uniprot.org/core/author"Glover J.N."xsd:string
http://purl.uniprot.org/citations/18842000http://purl.uniprot.org/core/author"Kleiman F.E."xsd:string
http://purl.uniprot.org/citations/18842000http://purl.uniprot.org/core/author"Kleiman F.E."xsd:string
http://purl.uniprot.org/citations/18842000http://purl.uniprot.org/core/author"Nazeer I."xsd:string
http://purl.uniprot.org/citations/18842000http://purl.uniprot.org/core/author"Nazeer I."xsd:string
http://purl.uniprot.org/citations/18842000http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18842000http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18842000http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/18842000http://purl.uniprot.org/core/name"Biochemistry"xsd:string