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J. Biol. Chem., Vol. 276, Issue 45, 41906-41912, November 9, 2001
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§,¶, and
**
From the Dmc1 and Rad51 are eukaryotic RecA homologues
that are involved in meiotic recombination. The expression of Dmc1 is
limited to meiosis, whereas Rad51 is expressed in mitosis and meiosis. Dmc1 and Rad51 have unique and overlapping functions during meiotic recombination. Here we report the purification of the Dmc1 protein from
the budding yeast Saccharomyces cerevisiae and present
basic characterization of its biochemical activity. The protein has a
weak DNA-dependent ATPase activity and binds both
single-strand DNA (ssDNA) and double-strand DNA. Electrophoretic
mobility shift assays suggest that DNA binding by Dmc1 is cooperative.
Dmc1 renatures linearized plasmid DNA with first order reaction
kinetics and without requiring added nucleotide cofactor. In addition,
Dmc1 catalyzes strand assimilation of ssDNA oligonucleotides into
homologous supercoiled duplex DNA in a reaction promoted by ATP or the
non-hydrolyzable ATP analogue AMP-PNP.
Department of Molecular Genetics and Cell
Biology and the Department of Radiation and Cellular Oncology,
University of Chicago, Chicago, Illinois 60637 and the
¶ Department of Biology, Graduate School of Science, Osaka
University, Toyonaka, Osaka 560-0043, Japan
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