Abstract
BRCA2 is an important tumor suppressor and functions in homologous recombination, a key genomic integrity pathway. BRCA2 interacts with RAD51, the central protein of recombination, which forms filaments on 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 RPA-covered ssDNA in a manner that is stimulated by DSS1.
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