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TitleBRCA1-BARD1 combines multiple chromatin recognition modules to bridge nascent nucleosomes.
Journal, issue, pagesNucleic Acids Res, Vol. 51, Issue 20, Page 11080-11103, Year 2023
Publish dateNov 10, 2023
AuthorsHayden Burdett / Martina Foglizzo / Laura J Musgrove / Dhananjay Kumar / Gillian Clifford / Lisa J Campbell / George R Heath / Elton Zeqiraj / Marcus D Wilson /
PubMed AbstractChromatin 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 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.
External linksNucleic Acids Res / PubMed:37823591 / PubMed Central
MethodsEM (single particle)
Resolution3.4 - 21.5 Å
Structure data

16859

8off

EMDB-16859, PDB-8off:
Structure of BARD1 ARD-BRCTs in complex with H2AKc15ub nucleosomes (Map1)
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-16869: Low-resolution structure of BRCA1dExon11-FL BARD1 (closed state)
Method: EM (single particle) / Resolution: 21.5 Å

EMDB-16870: Low-resolution structure of BRCA1dExon11-FL BARD1 (open state)
Method: EM (single particle) / Resolution: 18.4 Å

EMDB-17928: Structure of BARD1 ARD-BRCTs in complex with H2AKc15ub nucleosomes (Map 2)
Method: EM (single particle) / Resolution: 3.75 Å

Source
  • homo sapiens (human)
  • felis catus (domestic cat)
KeywordsDNA BINDING PROTEIN / BRCA1-BARD1 / chromatin recognition / nucleosomes / ubiquitin

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