Human BRCA2 protein promotes RAD51 filament formation on RPA-covered single-stranded DNA

Nat Struct Mol Biol. 2010 Oct;17(10):1260-2. doi: 10.1038/nsmb.1904. Epub 2010 Aug 22.

Abstract

BRCA2 is a tumor suppressor that functions in homologous recombination, a key genomic integrity pathway. BRCA2 interacts with RAD51, the central protein of recombination, which forms filaments on single-stranded DNA (ssDNA) to perform homology search and DNA strand invasion. We report the purification of full-length human BRCA2 and show that it binds to ~6 RAD51 molecules and promotes RAD51 binding to ssDNA coated by replication protein A (RPA), in a manner that is stimulated by DSS1.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Apoptosis Regulatory Proteins
  • BRCA2 Protein / chemistry
  • BRCA2 Protein / isolation & purification
  • BRCA2 Protein / physiology*
  • Chromatography, Affinity
  • DNA Repair / physiology
  • DNA, Circular / metabolism
  • DNA, Single-Stranded / metabolism*
  • Humans
  • Models, Biological
  • Proteasome Endopeptidase Complex / physiology
  • Protein Binding
  • Protein Interaction Mapping
  • Rad51 Recombinase / chemistry
  • Rad51 Recombinase / physiology*
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / isolation & purification
  • Recombinant Fusion Proteins / physiology
  • Recombination, Genetic / physiology
  • Replication Protein A

Substances

  • Apoptosis Regulatory Proteins
  • BLID protein, human
  • BRCA2 Protein
  • BRCA2 protein, human
  • DNA, Circular
  • DNA, Single-Stranded
  • Recombinant Fusion Proteins
  • Replication Protein A
  • SHFM1 protein, human
  • RAD51 protein, human
  • Rad51 Recombinase
  • Proteasome Endopeptidase Complex