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http://purl.uniprot.org/citations/37823591http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/37823591http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/37823591http://www.w3.org/2000/01/rdf-schema#comment"Chromatin association of the BRCA1-BARD1 heterodimer is critical to promote homologous recombination repair of DNA double-strand breaks (DSBs) in S/G2. How the BRCA1-BARD1 complex interacts with chromatin that contains both damage induced histone H2A ubiquitin and inhibitory H4K20 methylation is not fully understood. We characterised BRCA1-BARD1 binding and enzymatic activity to an array of mono- and di-nucleosome substrates using biochemical, structural and single molecule imaging approaches. We found that the BRCA1-BARD1 complex preferentially interacts and modifies di-nucleosomes over mono-nucleosomes, allowing integration of H2A Lys-15 ubiquitylation signals with other chromatin modifications and features. Using high speed-atomic force microscopy (HS-AFM) to monitor how the BRCA1-BARD1 complex recognises chromatin in real time, we saw a highly dynamic complex that bridges two nucleosomes and associates with the DNA linker region. Bridging is aided by multivalent cross-nucleosome interactions that enhance BRCA1-BARD1 E3 ubiquitin ligase catalytic activity. Multivalent interactions across nucleosomes explain how BRCA1-BARD1 can recognise chromatin that retains partial di-methylation at H4 Lys-20 (H4K20me2), a parental histone mark that blocks BRCA1-BARD1 interaction with nucleosomes, to promote its enzymatic and DNA repair activities."xsd:string
http://purl.uniprot.org/citations/37823591http://purl.org/dc/terms/identifier"doi:10.1093/nar/gkad793"xsd:string
http://purl.uniprot.org/citations/37823591http://purl.org/dc/terms/identifier"doi:10.1093/nar/gkad793"xsd:string
http://purl.uniprot.org/citations/37823591http://purl.uniprot.org/core/author"Burdett H."xsd:string
http://purl.uniprot.org/citations/37823591http://purl.uniprot.org/core/author"Burdett H."xsd:string
http://purl.uniprot.org/citations/37823591http://purl.uniprot.org/core/author"Kumar D."xsd:string
http://purl.uniprot.org/citations/37823591http://purl.uniprot.org/core/author"Kumar D."xsd:string
http://purl.uniprot.org/citations/37823591http://purl.uniprot.org/core/author"Wilson M.D."xsd:string
http://purl.uniprot.org/citations/37823591http://purl.uniprot.org/core/author"Wilson M.D."xsd:string
http://purl.uniprot.org/citations/37823591http://purl.uniprot.org/core/author"Zeqiraj E."xsd:string
http://purl.uniprot.org/citations/37823591http://purl.uniprot.org/core/author"Zeqiraj E."xsd:string
http://purl.uniprot.org/citations/37823591http://purl.uniprot.org/core/author"Campbell L.J."xsd:string
http://purl.uniprot.org/citations/37823591http://purl.uniprot.org/core/author"Campbell L.J."xsd:string
http://purl.uniprot.org/citations/37823591http://purl.uniprot.org/core/author"Clifford G."xsd:string
http://purl.uniprot.org/citations/37823591http://purl.uniprot.org/core/author"Clifford G."xsd:string
http://purl.uniprot.org/citations/37823591http://purl.uniprot.org/core/author"Foglizzo M."xsd:string
http://purl.uniprot.org/citations/37823591http://purl.uniprot.org/core/author"Foglizzo M."xsd:string
http://purl.uniprot.org/citations/37823591http://purl.uniprot.org/core/author"Heath G.R."xsd:string
http://purl.uniprot.org/citations/37823591http://purl.uniprot.org/core/author"Heath G.R."xsd:string
http://purl.uniprot.org/citations/37823591http://purl.uniprot.org/core/author"Musgrove L.J."xsd:string
http://purl.uniprot.org/citations/37823591http://purl.uniprot.org/core/author"Musgrove L.J."xsd:string
http://purl.uniprot.org/citations/37823591http://purl.uniprot.org/core/date"2023"xsd:gYear
http://purl.uniprot.org/citations/37823591http://purl.uniprot.org/core/date"2023"xsd:gYear