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Papers In Press, published online ahead of print June 19, 2002
J. Biol. Chem, 10.1074/jbc.M203494200
Submitted on April 11, 2002
Revised on June 7, 2002
Accepted on June 19, 2002
Section of Microbiology, University of California, Davis, Davis, CA 95616
Corresponding Author: sckowalczykowski{at}ucdavis.edu
The Rad51 nucleoprotein filament mediates DNA strand exchange, a key step of homologous recombination. This activity is stimulated by RPA, but only when RPA is introduced after Rad51 nucleoprotein filament formation. In contrast, RPA inhibits Rad51 nucleoprotein complex formation by prior binding to ssDNA, but Rad52 protein alleviates this inhibition. Here we show that Rad51 filament formation is simultaneous with displacement of RPA from ssDNA. This displacement is initiated by a rate-limiting nucleation of Rad51 protein onto ssDNA complex, followed by rapid elongation of the filament. Rad52 protein accelerates RPA displacement by Rad51 protein. This acceleration likely involves direct interactions with both Rad51 protein and RPA. Detection of a Rad52-RPA-ssDNA co-complex suggests that this co-complex is an intermediate in the displacement process.
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