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Three-Dimensional Architecture of the Human BRCA1-A Histone Deubiquitinase Core Complex.

Abstract：

:BRCA1 is a tumor suppressor found to be mutated in hereditary breast and ovarian cancer and plays key roles in the maintenance of genomic stability by homologous recombination repair. It is recruited to damaged chromatin as a component of the BRCA1-A deubiquitinase, which cleaves K63-linked ubiquitin chains attached to histone H2A and H2AX. BRCA1-A contributes to checkpoint regulation, repair pathway choice, and HR repair efficiency through molecular mechanisms that remain largely obscure. The structure of an active core complex comprising two Abraxas/BRCC36/BRCC45/MERIT40 tetramers determined by negative-stain electron microscopy (EM) reveals a distorted V-shape architecture in which a dimer of Abraxas/BRCC36 heterodimers sits at the base, with BRCC45/Merit40 pairs occupying each arm. The location and ubiquitin-binding activity of BRCC45 suggest that it may provide accessory interactions with nucleosome-linked ubiquitin chains that contribute to their efficient processing. Our data also suggest how ataxia telangiectasia mutated (ATM)-dependent BRCA1 dimerization may stabilize self-association of the entire BRCA1-A complex.

journal_name

Cell Rep

journal_title

Cell reports

authors

Kyrieleis OJP,McIntosh PB,Webb SR,Calder LJ,Lloyd J,Patel NA,Martin SR,Robinson CV,Rosenthal PB,Smerdon SJ

doi

10.1016/j.celrep.2016.11.063

subject

Has Abstract

pub_date

2016-12-20 00:00:00

pages

3099-3106

issue

12

issn

2211-1247

pii

S2211-1247(16)31637-0

journal_volume

17

pub_type

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