Bivalent recognition of histone marks by BARD1

Min Deng; Jing Hou; Zhenkun Lou

doi:10.1016/j.tcb.2021.06.005

Bivalent recognition of histone marks by BARD1

Trends Cell Biol. 2021 Sep;31(9):703-704. doi: 10.1016/j.tcb.2021.06.005. Epub 2021 Jun 29.

Authors

Min Deng¹, Jing Hou², Zhenkun Lou³

Affiliations

¹ State Key Laboratory of Molecular Oncology, National Cancer Center, National Clinical Research Center for Cancer, Cancer Hospital, Chinese Academy of Medical Sciences and Peking Union Medical College, 100021 Beijing, China; Department of Radiation Oncology, National Cancer Center, National Clinical Research Center for Cancer, Cancer Hospital, Chinese Academy of Medical Sciences and Peking Union Medical College, 100021 Beijing, China. Electronic address: dengmin@cicams.ac.cn.
² Department of Oncology, Mayo Clinic, Rochester, MN 55905, USA.
³ Department of Oncology, Mayo Clinic, Rochester, MN 55905, USA. Electronic address: Lou.Zhenkun@mayo.edu.

PMID: 34215490
DOI: 10.1016/j.tcb.2021.06.005

Abstract

BARD1 directs BRCA1 to DNA damage sites to facilitate homology recombination. Zhou and colleagues have now determined the cryo-electron microscopy (cryo-EM) structure of BARD1 bound to a nucleosome core particle with two marks: H2AK15ub and H4K20me0. The structure illustrates how bivalent recognition of both marks mediates highly specified recruitment of the BARD1-BRCA1 complex.

Keywords: BARD1; BRCA1; cryo-electron microscopy structure; homologous recombination; nucleosomes.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Cryoelectron Microscopy
Histone Code*
Histones* / metabolism
Humans
Tumor Suppressor Proteins / genetics
Tumor Suppressor Proteins / metabolism
Ubiquitin-Protein Ligases / metabolism

Substances

Histones
Tumor Suppressor Proteins
BARD1 protein, human
Ubiquitin-Protein Ligases