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TitleMechanisms of BRCA1-BARD1 nucleosome recognition and ubiquitylation.
Journal, issue, pagesNature, Vol. 596, Issue 7872, Page 438-443, Year 2021
Publish dateJul 28, 2021
AuthorsQi Hu / Maria Victoria Botuyan / Debiao Zhao / Gaofeng Cui / Elie Mer / Georges Mer /
PubMed AbstractThe BRCA1-BARD1 tumour suppressor is an E3 ubiquitin ligase necessary for the repair of DNA double-strand breaks by homologous recombination. The BRCA1-BARD1 complex localizes to damaged chromatin ...The BRCA1-BARD1 tumour suppressor is an E3 ubiquitin ligase necessary for the repair of DNA double-strand breaks by homologous recombination. The BRCA1-BARD1 complex localizes to damaged chromatin after DNA replication and catalyses the ubiquitylation of histone H2A and other cellular targets. The molecular bases for the recruitment to double-strand breaks and target recognition of BRCA1-BARD1 remain unknown. Here we use cryo-electron microscopy to show that the ankyrin repeat and tandem BRCT domains in BARD1 adopt a compact fold and bind to nucleosomal histones, DNA and monoubiquitin attached to H2A amino-terminal K13 or K15, two signals known to be specific for double-strand breaks. We further show that RING domains in BRCA1-BARD1 orient an E2 ubiquitin-conjugating enzyme atop the nucleosome in a dynamic conformation, primed for ubiquitin transfer to the flexible carboxy-terminal tails of H2A and variant H2AX. Our work reveals a regulatory crosstalk in which recognition of monoubiquitin by BRCA1-BARD1 at the N terminus of H2A blocks the formation of polyubiquitin chains and cooperatively promotes ubiquitylation at the C terminus of H2A. These findings elucidate the mechanisms of BRCA1-BARD1 chromatin recruitment and ubiquitylation specificity, highlight key functions of BARD1 in both processes and explain how BRCA1-BARD1 promotes homologous recombination by opposing the DNA repair protein 53BP1 in post-replicative chromatin. These data provide a structural framework to evaluate BARD1 variants and help to identify mutations that drive the development of cancer.
External linksNature / PubMed:34321665 / PubMed Central
MethodsEM (single particle)
Resolution2.91 - 3.28 Å
Structure data

23590

7lya

EMDB-23590, PDB-7lya:
Cryo-EM structure of the human nucleosome core particle with linked histone proteins H2A and H2B
Method: EM (single particle) / Resolution: 2.91 Å

23591

7lyb

EMDB-23591, PDB-7lyb:
Cryo-EM structure of the human nucleosome core particle in complex with BRCA1-BARD1-UbcH5c
Method: EM (single particle) / Resolution: 3.28 Å

23592

7lyc

EMDB-23592, PDB-7lyc:
Cryo-EM structure of the human nucleosome core particle ubiquitylated at histone H2A Lys13 and Lys15 in complex with BARD1 (residues 415-777)
Method: EM (single particle) / Resolution: 2.94 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsSTRUCTURAL PROTEIN/DNA / Nucleosome core particle / chromatin / DNA replication / DNA repair / STRUCTURAL PROTEIN-DNA complex / BRCA1 / BARD1 / UbcH5c / DNA double-strand break / Homologous recombination / 53BP1 / ARD domain / Ankyrine repeat domain / Tandem BRCT domain / ubiquitin

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