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Papers In Press, published online ahead of print February 3, 2003
Section of Microbiology, University of California, Davis, Davis, CA 95616
Corresponding Author: sckowalczykowski{at}ucdavis.edu
Homologous recombination is important for the repair of double-stranded DNA breaks in all organisms. Rad51 and Rad54 proteins are two key components of the homologous recombination machinery in eukaryotes. In vitro, Rad51 protein assembles with single-stranded (ss) DNA to form the helical nucleoprotein filament that promotes DNA strand exchange, a basic step of homologous recombination. Rad54 protein interacts with this Rad51 nucleoprotein filament and stimulates its DNA pairing activity, suggesting that Rad54 protein is a component of the nucleoprotein complex involved in the DNA homology search. Here, using physical criteria, we demonstrate directly the formation of Rad54-Rad51-DNA nucleoprotein co-complexes that contain equimolar amounts of each protein. The binding of Rad54 protein significantly stabilizes the Rad51 nucleoprotein filament formed on either ssDNA or double-stranded (ds) DNA. The Rad54-stabilized nucleoprotein filament is more competent in DNA strand exchange, and acts over a broader range of solution conditions. Thus, the co-assembly of an interacting partner with the Rad51 nucleoprotein filament represents a novel means of stabilizing the biochemical entity central to homologous recombination, and reveals a new function of Rad54 protein.
J. Biol. Chem, 10.1074/jbc.M212779200
Submitted on December 16, 2002
Revised on February 3, 2003
Accepted on February 3, 2003
A novel function of RAD54 protein: Stabilization of the RAD51 nucleoprotein filament
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