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J. Biol. Chem., Vol. 275, Issue 43, 33782-33790, October 27, 2000
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From the Departments of RecA and Rad51 proteins are essential for
homologous recombination in Bacteria and
Eukarya, respectively. Homologous proteins, called RadA,
have been described for Archaea. Here we present the
characterization of two RecA/Rad51 family proteins, RadA and RadB, from
Pyrococcus furiosus. The radA and
radB genes were not induced by DNA damage resulting from
exposure of the cells to Molecular Biology and
§ Structural Biology, Biomolecular Engineering Research
Institute, Suita, Osaka 565-0874, Japan, the ¶ Center of Marine
Biotechnology, University of Maryland Biotechnology Institute,
Baltimore, Maryland 21202, and the Department of
Molecular Microbiology, Research Institute for Microbial Diseases,
Osaka University, Suita, Osaka 565-0871, Japan
and UV irradiation and heat shock,
suggesting that they might be constitutively expressed in this
hyperthermophile. RadA had DNA-dependent ATPase, D-loop
formation, and strand exchange activities. In contrast, RadB had a very
weak ATPase activity that is not stimulated by DNA. This protein had a
strong binding affinity for DNA, but little strand exchange activity
could be detected. A direct interaction between RadA and RadB was
detected by an immunoprecipitation assay. Moreover, RadB, but not RadA,
coprecipitated with Hjc, a Holliday junction resolvase found in
P. furiosus, in the absence of ATP. This interaction was
suppressed in the presence of ATP. The Holliday junction cleavage
activity of Hjc was inhibited by RadB in the absence, but not in the
presence, of ATP. These results suggest that RadB has important roles
in homologous recombination in Archaea and may regulate the
cleavage reactions of the branch-structured DNA.
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