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J. Biol. Chem., Vol. 278, Issue 16, 14029-14036, April 18, 2003
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§,
From the 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 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 single-stranded DNA or double-stranded 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.
Department of Biochemistry, Drexel
University College of Medicine, Philadelphia, Pennsylvania 19102-1192 and the § Division of Biological Sciences, Sections of
Microbiology and of Molecular and Cellular Biology, University of
California, Davis, California 95616-8665
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