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J. Biol. Chem., Vol. 279, Issue 29, 30385-30394, July 16, 2004

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hXRCC2 Enhances ADP/ATP Processing and Strand Exchange by hRAD51^*

Kang Sup Shim, Christoph Schmutte, Gregory Tombline, Christopher D. Heinen, and Richard Fishel

From the Genetics and Molecular Biology Program, Department of Microbiology and Immunology, Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, Pennsylvania 19107

The assembly of bacterial RecA, and its human homolog hRAD51, into an operational ADP/ATP-regulated DNA-protein (nucleoprotein) filament is essential for homologous recombination repair (HRR). Yet hRAD51 lacks the coordinated ADP/ATP processing exhibited by RecA and is less efficient in HRR reactions in vitro. In this study, we demonstrate that hXRCC2, one of five other poorly understood non-redundant human mitotic RecA homologs (hRAD51B, hRAD51C, hRAD51D, hXRCC2, and hXRCC3), stimulates hRAD51 ATP processing. hXRCC2 also increases hRAD51-mediated DNA unwinding and strand exchange activities that are integral for HRR. Although there does not seem to be a long-lived interaction between hXRCC2 and hRAD51, we detail a strong adenosine nucleotide-regulated interaction between the hXRCC2-hRAD51D heterodimer and hRAD51. These observations begin to elucidate the separate and specialized functions of the human mitotic RecA homologs that enable an efficient nucleoprotein filament required for HRR.

Received for publication, June 9, 2003 , and in revised form, April 29, 2004.

^* This work was supported by National Institutes of Health Grant CA56542 and Department of Defense Grant DAMD17-99-1-9406. 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.

To whom correspondence should be addressed: Kimmel Cancer Center–BLSB933, 233 S. 10th St., Philadelphia, PA 19107. Tel.: 215-503-1345; Fax: 215-503-6739; E-mail: rfishel{at}lac.jci.tju.edu.

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