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M601249200v1
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Papers In Press, published online ahead of print March 2, 2006
J. Biol. Chem, 10.1074/jbc.M601249200
Submitted on February 8, 2006
Revised on March 1, 2006
Accepted on March 2, 2006

Recombination mediator and RAD51 targeting activities of a human BRCA2 polypeptide

Joseph San Filippo, Peter Chi, Michael G. Sehorn, Julia Etchin, Lumir Krejci, and Patrick Sung

Molecular Biophysics & Biochemistry, Yale University, New Haven, CT 06520

Corresponding Author: patrick.sung{at}yale.edu

BRCA2 likely exerts its tumor suppressor function by enhancing the efficiency of the homology-directed repair of injured chromosomes. To help define the DNA repair role of BRCA2, we have expressed and purified a polypeptide, BRC3/4-DBD, that harbors its BRC3 and BRC4 repeats and DNA binding domain. BRC3/4-DBD interacts with hRad51 and binds DNA with a distinct preference for ssDNA. Importantly, we demonstrate by biochemical means and electron microscopy that BRC3/4-DBD nucleates hRad51 onto ssDNA and acts as a recombination mediator in enabling hRad51 to utilize RPA-coated ssDNA as recombination substrate. These functions of BRC3/4-DBD require both the BRC repeats and the BRCA2 DNA binding domain. The results thus clarify the role of BRCA2 in Rad51-dependent DNA recombination and repair, and the experimental strategies described herein should be valuable for systematically deciphering this BRCA2 function.


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