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J. Biol. Chem., Vol. 277, Issue 48, 46205-46215, November 29, 2002
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From the Rad54 protein is a Snf2-like ATPase with a
specialized function in the recombinational repair of DNA damage. Rad54
is thought to stimulate the search of homology via formation of a
specific complex with the presynaptic Rad51 filament on
single-stranded DNA. Herein, we address the interaction of Rad54
with Rad51 filaments on double-stranded (ds) DNA, an intermediate in
DNA strand exchange with unclear functional significance. We show that
Saccharomyces cerevisiae Rad54 exerts distinct modes of
ATPase activity on partially and fully saturated filaments of Rad51
protein on dsDNA. The highest ATPase activity is observed on dsDNA
containing short patches of yeast Rad51 filaments resulting in a 6-fold
increase compared with protein-free DNA. This enhanced ATPase mode of
yeast Rad54 can also be elicited by partial filaments of human Rad51
protein but to a lesser extent. In contrast, the interaction of Rad54 protein with duplex DNA fully covered with Rad51 is entirely
species-specific. When yeast Rad51 fully covers dsDNA, Rad54 protein
hydrolyzes ATP in a reduced mode at 60-80% of its rate on
protein-free DNA. Instead, saturated filaments with human Rad51 fail to
support the yeast Rad54 ATPase. We suggest that the interaction of
Rad54 with dsDNA-Rad51 complexes is of functional importance in
homologous recombination.
Division of Biological Sciences, Section of
Microbiology and § Section of Molecular and Cellular
Biology, Center for Genetics and Development, University of California,
Davis, California 95616-8665
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