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J. Biol. Chem., Vol. 279, Issue 50, 51973-51980, December 10, 2004

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Multiple Interactions with the Rad51 Recombinase Govern the Homologous Recombination Function of Rad54^*

Markus Raschle, Stephen Van Komen¶, Peter Chi¶, Tom Ellenberger||, and Patrick Sung¶**

From the Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115-5730 and the ^¶Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06520

In eukaryotes, Rad51 and Rad54 functionally cooperate to mediate homologous recombination and the repair of damaged chromosomes by recombination. Rad51, the eukaryotic counterpart of the bacterial RecA recombinase, forms filaments on single-stranded DNA that are capable of pairing the bound DNA with a homologous double-stranded donor to yield joint molecules. Rad54 enhances the homologous DNA pairing reaction, and this stimulatory effect involves a physical interaction with Rad51. Correspondingly, the ability of Rad54 to hydrolyze ATP and introduce superhelical tension into covalently closed circular plasmid DNA is stimulated by Rad51. By controlled proteolysis, we show that the amino-terminal region of yeast Rad54 is rather unstructured. Truncation mutations that delete the N-terminal 113 or 129 amino acid residues of Rad54 attenuate or ablate physical and functional interactions with Rad51 under physiological ionic strength, respectively. Surprisingly, under less stringent conditions, the Rad54 129 protein can interact with Rad51 in affinity pull-down and functional assays. These results highlight the functional importance of the N-terminal Rad51 interaction domain of Rad54 and reveal that Rad54 contacts Rad51 through separable epitopes.

Received for publication, September 2, 2004 , and in revised form, September 28, 2004.

^* This work was supported in part by Department of Energy Grant DE-FG02-01E263071 and National Institutes of Health (NIH) Grant GM52504 (to T. E.) and NIH Grants ES07061 and GM57814 (to P. S.). 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.

These authors contributed equally to this work.

^|| The Hsien Wu and Daisy Yen Wu Professor at Harvard Medical School. To whom correspondence may be addressed: Dept. of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Ave., Boston, MA 02115-5730. Tel.: 617-432-0458; Fax: 617-432-3880; E-mail: tome{at}hms.harvard.edu. ** To whom correspondence may be addressed: Dept. of Molecular Biophysics and Biochemistry, Yale University School of Medicine, 333 Cedar St., C130 Sterling Hall of Medicine, New Haven, CT 06520. Tel.: 203-785-4552; Fax: 203-785-6404; E-mail: Patrick.Sung{at}yale.edu.

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