Structure of a meiosis-specific complex central to BRCA2 localization at recombination sites

Pendlebury, Devon F.; Zhang, Jingjing; Agrawal, Ritvija; Shibuya, Hiroki; Nandakumar, Jayakrishnan

doi:10.1038/s41594-021-00635-0

Structure of a meiosis-specific complex central to BRCA2 localization at recombination sites

Journal Article · 01 August 2021 · Nat. Struct. Mol. Biol.

DOI:https://doi.org/10.1038/s41594-021-00635-0· OSTI ID:1814808

Pendlebury, Devon F.; Zhang, Jingjing; Agrawal, Ritvija; Shibuya, Hiroki; Nandakumar, Jayakrishnan

Research Organization:: Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Organization:: DOE - Office Of Science; National Institutes of Health (NIH)

OSTI ID:: 1814808

Journal Information:: Nat. Struct. Mol. Biol., Vol. 28

Country of Publication:: United States

Language:: ENGLISH

References (23)

Emerging functions of BRCA2 in DNA recombination No authors listed Trends in Biochemical Sciences https://doi.org/10.1016/j.tibs.2004.04.009		June 2004
The BRCA Tumor Suppressor Network in Chromosome Damage Repair by Homologous Recombination No authors listed Annual Review of Biochemistry https://doi.org/10.1146/annurev-biochem-013118-111058		June 2019
Links between genome integrity and BRCA1 tumor suppression No authors listed Trends in Biochemical Sciences https://doi.org/10.1016/j.tibs.2012.06.007		October 2012
Breast and Ovarian Cancer No authors listed New England Journal of Medicine https://doi.org/10.1056/NEJMra012284		June 2003
The MRE11 complex: starting from the ends No authors listed Nature Reviews Molecular Cell Biology https://doi.org/10.1038/nrm3047		January 2011
The TopoVIB-Like protein family is required for meiotic DNA double-strand break formation No authors listed Science https://doi.org/10.1126/science.aad5309		February 2016
A meiosis-specific BRCA2 binding protein recruits recombinases to DNA double-strand breaks to ensure homologous recombination No authors listed Nature Communications https://doi.org/10.1038/s41467-019-08676-2		February 2019
The BRCA2-MEILB2-BRME1 complex governs meiotic recombination and impairs the mitotic BRCA2-RAD51 function in cancer cells No authors listed Nature Communications https://doi.org/10.1038/s41467-020-15954-x		April 2020
HSF2BP Interacts with a Conserved Domain of BRCA2 and Is Required for Mouse Spermatogenesis No authors listed Cell Reports https://doi.org/10.1016/j.celrep.2019.05.096		June 2019
Inference of Macromolecular Assemblies from Crystalline State No authors listed Journal of Molecular Biology https://doi.org/10.1016/j.jmb.2007.05.022		September 2007
Structure and mechanism of action of the BRCA2 breast cancer tumor suppressor No authors listed Nature Structural & Molecular Biology https://doi.org/10.1038/nsmb.2899		October 2014
Crystal structure of nerve growth factor in complex with the ligand-binding domain of the TrkA receptor No authors listed Nature https://doi.org/10.1038/43705		September 1999
Protein domains correlate strongly with exons in multiple eukaryotic genomes – evidence of exon shuffling? No authors listed Trends in Genetics https://doi.org/10.1016/j.tig.2004.06.013		September 2004
MEIOB Targets Single-Strand DNA and Is Necessary for Meiotic Recombination No authors listed PLoS Genetics https://doi.org/10.1371/journal.pgen.1003784		September 2013
MEIOB exhibits single-stranded DNA-binding and exonuclease activities and is essential for meiotic recombination No authors listed Nature Communications https://doi.org/10.1038/ncomms3788		November 2013
Genetic evidence suggests that Spata22 is required for the maintenance of Rad51 foci in mammalian meiosis No authors listed Scientific Reports https://doi.org/10.1038/srep06148		August 2014
Ulp1-SUMO Crystal Structure and Genetic Analysis Reveal Conserved Interactions and a Regulatory Element Essential for Cell Growth in Yeast No authors listed Molecular Cell https://doi.org/10.1016/S1097-2765(00)80326-3		May 2000
Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein No authors listed Science https://doi.org/10.1126/science.1279805		November 1992
XDS No authors listed Acta Crystallographica Section D Biological Crystallography https://doi.org/10.1107/S0907444909047337		January 2010
Integration, scaling, space-group assignment and post-refinement No authors listed Acta Crystallographica Section D Biological Crystallography https://doi.org/10.1107/S0907444909047374		January 2010
PHENIX: a comprehensive Python-based system for macromolecular structure solution No authors listed Acta Crystallographica Section D Biological Crystallography https://doi.org/10.1107/S0907444909052925		January 2010
Coot model-building tools for molecular graphics No authors listed Acta Crystallographica Section D Biological Crystallography https://doi.org/10.1107/S0907444904019158		November 2004
Towards automated crystallographic structure refinement with phenix.refine No authors listed Acta Crystallographica Section D Biological Crystallography https://doi.org/10.1107/S0907444912001308		March 2012

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