Insights into DNA recombination from the structure of a RAD51–BRCA2 complex

Luca Pellegrini, David S. Yu, Thomas Lo, Shubha Anand, MiYoung Lee, Tom L. Blundell and Ashok R. Venkitaraman ()
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Luca Pellegrini: University of Cambridge
David S. Yu: University of Cambridge, CR UK Department of Oncology and The Medical Research Council Cancer Cell Unit, Hutchison/MRC Research Centre
Thomas Lo: University of Cambridge
Shubha Anand: University of Cambridge, CR UK Department of Oncology and The Medical Research Council Cancer Cell Unit, Hutchison/MRC Research Centre
MiYoung Lee: University of Cambridge, CR UK Department of Oncology and The Medical Research Council Cancer Cell Unit, Hutchison/MRC Research Centre
Tom L. Blundell: University of Cambridge
Ashok R. Venkitaraman: University of Cambridge, CR UK Department of Oncology and The Medical Research Council Cancer Cell Unit, Hutchison/MRC Research Centre

Nature, 2002, vol. 420, issue 6913, 287-293

Abstract: Abstract The breast cancer susceptibility protein BRCA2 controls the function of RAD51, a recombinase enzyme, in pathways for DNA repair by homologous recombination. We report here the structure of a complex between an evolutionarily conserved sequence in BRCA2 (the BRC repeat) and the RecA-homology domain of RAD51. The BRC repeat mimics a motif in RAD51 that serves as an interface for oligomerization between individual RAD51 monomers, thus enabling BRCA2 to control the assembly of the RAD51 nucleoprotein filament, which is essential for strand-pairing reactions during DNA recombination. The RAD51 oligomerization motif is highly conserved among RecA-like recombinases, highlighting a common evolutionary origin for the mechanism of nucleoprotein filament formation, mirrored in the BRC repeat. Cancer-associated mutations that affect the BRC repeat disrupt its predicted interaction with RAD51, yielding structural insight into mechanisms for cancer susceptibility.

Date: 2002
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DOI: 10.1038/nature01230

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