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J. Biol. Chem., Vol. 277, Issue 17, 14417-14425, April 26, 2002
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From the Genetics and Molecular Biology Program, Department of
Microbiology and Immunology, Kimmel Cancer Center, Thomas Jefferson
University, Philadelphia, Pennsylvania 19107
The prototypical bacterial RecA protein promotes
recombination/repair by catalyzing strand exchange between homologous
DNAs. While the mechanism of strand exchange remains enigmatic,
ATP-induced cooperativity between RecA protomers is critical for its
function. A human RecA homolog, human RAD51 protein (hRAD51),
facilitates eukaryotic recombination/repair, although its ability to
hydrolyze ATP and/or promote strand exchange appears distinct from the
bacterial RecA. We have quantitatively examined the hRAD51 ATPase. The
catalytic efficiency
(kcat/Km) of the hRAD51
ATPase was ~50-fold lower than the RecA ATPase. Altering the ratio of
DNA/hRAD51 and including salts that stimulate DNA strand exchange
(ammonium sulfate and spermidine) were found to affect the catalytic
efficiency of hRAD51. The average site size of hRAD51 was determined to
be ~3 nt (bp) for both single-stranded and double-stranded DNA.
Importantly, hRAD51 lacks the magnitude of ATP-induced cooperativity
that is a hallmark of RecA. Together, these results suggest that hRAD51 may be unable to coordinate ATP hydrolysis between neighboring protomers.
To whom correspondence and reprint requests should be addressed:
Kimmel Cancer Center, BLSB 933, 233 S. 10th St., Philadelphia, PA
19107. Tel.: 213-503-1346; Fax: 215-923-1098; E-mail: rfishel@lac. jci.tju.edu.
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