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Originally published In Press as doi:10.1074/jbc.M004557200 on July 19, 2000

J. Biol. Chem., Vol. 275, Issue 43, 33782-33790, October 27, 2000
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Both RadA and RadB Are Involved in Homologous Recombination in Pyrococcus furiosus*

Kayoko KomoriDagger , Tomoko Miyata§, Jocelyne DiRuggiero, Rhonda Holley-Shanks, Ikuko HayashiDagger , Isaac K. O. CannDagger , Kota Mayanagi§, Hideo Shinagawa||, and Yoshizumi IshinoDagger **

From the Departments of Dagger  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

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 gamma  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.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

** To whom correspondence should be addressed: Dept. of Molecular Biology, Biomolecular Engineering Research Institute, 6-2-3 Furuedai, Suita, Osaka 565-0874, Japan. Tel.: 81-6-6872-8203; Fax: 81-6-6872-8219; E-mail: ishino@beri.co.jp.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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