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TitleStructural insight into BRCA1-BARD1 complex recruitment to damaged chromatin.
Journal, issue, pagesMol Cell, Vol. 81, Issue 13, Page 2765-22777.e6, Year 2021
Publish dateJul 1, 2021
AuthorsLinchang Dai / Yaxin Dai / Jinhua Han / Yan Huang / Longge Wang / Jun Huang / Zheng Zhou /
PubMed AbstractThe BRCA1-BARD1 complex directs the DNA double-strand break (DSB) repair pathway choice to error-free homologous recombination (HR) during the S-G2 stages. Targeting BRCA1-BARD1 to DSB-proximal sites ...The BRCA1-BARD1 complex directs the DNA double-strand break (DSB) repair pathway choice to error-free homologous recombination (HR) during the S-G2 stages. Targeting BRCA1-BARD1 to DSB-proximal sites requires BARD1-mediated nucleosome interaction and histone mark recognition. Here, we report the cryo-EM structure of BARD1 bound to a ubiquitinated nucleosome core particle (NCP) at 3.1 Å resolution and illustrate how BARD1 simultaneously recognizes the DNA damage-induced mark H2AK15ub and DNA replication-associated mark H4K20me0 on the nucleosome. In vitro and in vivo analyses reveal that the BARD1-NCP complex is stabilized by BARD1-nucleosome interaction, BARD1-ubiquitin interaction, and BARD1 ARD domain-BARD1 BRCT domain interaction, and abrogating these interactions is detrimental to HR activity. We further identify multiple disease-causing BARD1 mutations that disrupt BARD1-NCP interactions and hence impair HR. Together, this study elucidates the mechanism of BRCA1-BARD1 complex recruitment and retention by DSB-flanking nucleosomes and sheds important light on cancer therapeutic avenues.
External linksMol Cell / PubMed:34102105
MethodsEM (single particle)
Resolution3.1 Å
Structure data

31020

7e8i

EMDB-31020, PDB-7e8i:
Structural insight into BRCA1-BARD1 complex recruitment to damaged chromatin
Method: EM (single particle) / Resolution: 3.1 Å

Source
  • homo sapiens (human)
  • xenopus laevis (African clawed frog)
KeywordsNUCLEAR PROTEIN / BRCA1 / nucleosome / DNA damage / chromatin / BARD1

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