BRCA1/BARD1 intrinsically disordered regions facilitate chromatin recruitment and ubiquitylation.


Journal

The EMBO journal
ISSN: 1460-2075
Titre abrégé: EMBO J
Pays: England
ID NLM: 8208664

Informations de publication

Date de publication:
01 08 2023
Historique:
revised: 10 04 2023
received: 19 01 2023
accepted: 22 05 2023
pmc-release: 12 06 2024
medline: 3 8 2023
pubmed: 12 6 2023
entrez: 12 6 2023
Statut: ppublish

Résumé

BRCA1/BARD1 is a tumor suppressor E3 ubiquitin (Ub) ligase with roles in DNA damage repair and in transcriptional regulation. BRCA1/BARD1 RING domains interact with nucleosomes to facilitate mono-ubiquitylation of distinct residues on the C-terminal tail of histone H2A. These enzymatic domains constitute a small fraction of the heterodimer, raising the possibility of functional chromatin interactions involving other regions such as the BARD1 C-terminal domains that bind nucleosomes containing the DNA damage signal H2A K15-Ub and H4 K20me0, or portions of the expansive intrinsically disordered regions found in both subunits. Herein, we reveal novel interactions that support robust H2A ubiquitylation activity mediated through a high-affinity, intrinsically disordered DNA-binding region of BARD1. These interactions support BRCA1/BARD1 recruitment to chromatin and sites of DNA damage in cells and contribute to their survival. We also reveal distinct BRCA1/BARD1 complexes that depend on the presence of H2A K15-Ub, including a complex where a single BARD1 subunit spans adjacent nucleosome units. Our findings identify an extensive network of multivalent BARD1-nucleosome interactions that serve as a platform for BRCA1/BARD1-associated functions on chromatin.

Identifiants

pubmed: 37305927
doi: 10.15252/embj.2023113565
pmc: PMC10390874
doi:

Substances chimiques

Nucleosomes 0
Tumor Suppressor Proteins 0
BRCA1 Protein 0
Histones 0
Ubiquitin-Protein Ligases EC 2.3.2.27
Chromatin 0

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

e113565

Subventions

Organisme : NIGMS NIH HHS
ID : R01 GM141091
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA260834
Pays : United States
Organisme : NICHD NIH HHS
ID : R00 HD090201
Pays : United States
Organisme : NIGMS NIH HHS
ID : P41 GM103533
Pays : United States

Informations de copyright

© 2023 The Authors.

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Auteurs

Samuel R Witus (SR)

Department of Biochemistry, University of Washington, Seattle, WA, USA.

Lisa M Tuttle (LM)

Department of Biochemistry, University of Washington, Seattle, WA, USA.

Wenjing Li (W)

Department of Biochemistry and Structural Biology, University of Texas Health Science Center at San Antonio, San Antonio, TX, USA.

Alex Zelter (A)

Department of Biochemistry, University of Washington, Seattle, WA, USA.

Meiling Wang (M)

Department of Biochemistry and Structural Biology, University of Texas Health Science Center at San Antonio, San Antonio, TX, USA.

Klaiten E Kermoade (KE)

Department of Biochemistry, University of Washington, Seattle, WA, USA.

Damien B Wilburn (DB)

Department of Genome Sciences, University of Washington, Seattle, WA, USA.
Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.

Trisha N Davis (TN)

Department of Biochemistry, University of Washington, Seattle, WA, USA.

Peter S Brzovic (PS)

Department of Biochemistry, University of Washington, Seattle, WA, USA.

Weixing Zhao (W)

Department of Biochemistry and Structural Biology, University of Texas Health Science Center at San Antonio, San Antonio, TX, USA.

Rachel E Klevit (RE)

Department of Biochemistry, University of Washington, Seattle, WA, USA.

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Classifications MeSH