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J. Biol. Chem., Vol. 280, Issue 1, 722-728, January 7, 2005

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Crystal Structure of an ATPase-active Form of Rad51 Homolog from Methanococcus voltae

INSIGHTS INTO POTASSIUM DEPENDENCE^*

Yan Wu, Xinguo Qian, Yujiong He, Ignace A. Moya, and Yu Luo

From the Department of Biochemistry, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5E5, Canada

Homologous gene recombination is crucial for the repair of DNA. A superfamily of recombinases facilitate a central strand exchange reaction in the repair process. This reaction is initiated by coating single-stranded DNA (ssDNA) with recombinases in the presence of ATP and Mg²⁺ co-factors to form helical nucleoprotein filaments with elevated ATPase and strand invasion activities (1). At the amino acid sequence level, archaeal RadA and Rad51 and eukaryal Rad51 and meiosis-specific DMC1 form a closely related group of recombinases distinct from bacterial RecA (2). Unlike the extensively studied Escherichia coli RecA (EcRecA), increasing evidences on yeast and human recombinases imply that their optimal activities are dependent on the presence of a monovalent cation, particularly potassium (3-5). Here we present the finding that archaeal RadA from Methanococcus voltae (MvRadA) is a stringent potassium-dependent ATPase, and the crystal structure of this protein in complex with the non-hydrolyzable ATP analog adenosine 5'-(,-iminotriphosphate), Mg²⁺, and K⁺ at 2.4 Å resolution. Potassium triggered an in situ conformational change in the ssDNA-binding L2 region concerted with incorporation of two potassium ions at the ATPase site in the RadA crystals preformed in K⁺-free medium. Both potassium ions were observed in contact with the -phosphate of the ATP analog, implying a direct role by the monovalent cations in stimulating the ATPase activity. Cross-talk between the ATPase site and the ssDNA-binding L2 region visualized in the MvRadA structure provides an explanation to the co-factor-induced allosteric effect on RecA-like recombinases.

Received for publication, September 27, 2004 , and in revised form, October 27, 2004.

The atomic coordinates and structure factors (code 1XU4) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported in part by the Natural Sciences and Engineering Research Council of Canada, the Saskatchewan Health Research Foundation (SHRF), and the Canadian Institute of Health Research (CIHR) (all to Y. L.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

A CIHR/SHRF new investigator. To whom correspondence should be addressed.

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