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Division of Biological Sciences, Sections of Microbiology and of
Molecular and Cellular Biology,
1 Microbiology Graduate Group,
2 Genetics Graduate Group, University of California,
Davis, California 95616 USA
The Rad51 protein of Saccharomyces cerevisiae is a
eukaryotic homolog of the RecA protein, the prototypic DNA
strand-exchange protein of Escherichia coli. RAD51 gene
function is required for efficient genetic recombination and for DNA
double-strand break repair. Recently, we demonstrated that RecA protein
has a preferential affinity for GT-rich DNA sequences
several of which
exhibit enhanced RecA protein-promoted homologous pairing activity. The
fundamental similarity between the RecA and Rad51 proteins suggests
that Rad51 might display an analogous bias. Using in vitro selection,
here we show that the yeast Rad51 protein shares the same preference for GT-rich sequences as its prokaryotic counterpart. This bias is also
manifest as an increased ability of Rad51 protein to promote the
invasion of supercoiled DNA by homologous GT-rich single-stranded DNA,
an activity not previously described for the eukaryotic pairing protein. We propose that the preferred utilization of GT-rich sequences
is a conserved feature among all homologs of RecA protein, and that
GT-rich regions are loci for increased genetic exchange in both
prokaryotes and eukaryotes.
[Key Words: Rad51 protein; in vitro selection; genetic recombination; homologous pairing; genetic instability]
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