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

Min Deng, Jing Hou, Zhenkun Lou

Oncology

Research output: Contribution to journal › Short survey › peer-review

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.

Original language	English (US)
Pages (from-to)	703-704
Number of pages	2
Journal	Trends in Cell Biology
Volume	31
Issue number	9
DOIs	https://doi.org/10.1016/j.tcb.2021.06.005
State	Published - Sep 2021

Keywords

BARD1
BRCA1
cryo-electron microscopy structure
homologous recombination
nucleosomes

ASJC Scopus subject areas

Cell Biology

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10.1016/j.tcb.2021.06.005

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title = "Bivalent recognition of histone marks by BARD1",

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",

author = "Min Deng and Jing Hou and Zhenkun Lou",

note = "Publisher Copyright: {\textcopyright} 2021 Elsevier Ltd",

year = "2021",

month = sep,

doi = "10.1016/j.tcb.2021.06.005",

language = "English (US)",

volume = "31",

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AU - Deng, Min

AU - Hou, Jing

AU - Lou, Zhenkun

PY - 2021/9

Y1 - 2021/9

N2 - 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.

AB - 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.

KW - BARD1

KW - BRCA1

KW - cryo-electron microscopy structure

KW - homologous recombination

KW - nucleosomes

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U2 - 10.1016/j.tcb.2021.06.005

DO - 10.1016/j.tcb.2021.06.005

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SN - 0962-8924

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SP - 703

EP - 704

JO - Trends in Cell Biology

JF - Trends in Cell Biology

IS - 9

ER -

Bivalent recognition of histone marks by BARD1

Abstract

Keywords

ASJC Scopus subject areas

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