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Originally published In Press as doi:10.1074/jbc.M800839200 on July 10, 2008

J. Biol. Chem., Vol. 283, Issue 36, 24698-24706, September 5, 2008
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Rad51 Protein Stimulates the Branch Migration Activity of Rad54 Protein*Formula

Matthew J. Rossi and Alexander V. Mazin1

From the Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, Pennsylvania 19102-1192

The Rad51 and Rad54 proteins play important roles during homologous recombination in eukaryotes. Rad51 forms a nucleoprotein filament on single-stranded DNA and performs the initial steps of double strand break repair. Rad54 belongs to the Swi2/Snf2 family of ATP-dependent DNA translocases. We previously showed that Rad54 promotes branch migration of Holliday junctions. Here we find that human Rad51 (hRad51) significantly stimulates the branch migration activity of hRad54. The stimulation appears to be evolutionarily conserved, as yeast Rad51 also stimulates the branch migration activity of yeast Rad54. We further investigated the mechanism of this stimulation. Our results demonstrate that the stimulation of hRad54-promoted branch migration by hRad51 is driven by specific protein-protein interactions, and the active form of the hRad51 filament is more stimulatory than the inactive one. The current results support the hypothesis that the hRad51 conformation state has a strong effect on interaction with hRad54 and ultimately on the function of hRad54 in homologous recombination.


Received for publication, January 31, 2008 , and in revised form, June 10, 2008.

* This work was supported, in whole or in part, by National Institutes of Health Grants CA100839 and MH084119. This work was also supported by the Leukemia and Lymphoma Society Scholar Award 1054-09 (to A. V. M.). 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.

Formula The on-line version of this article (available at http://www.jbc.org) contains supplemental Table S1.

1 To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, Drexel University College of Medicine, 245 N 15th St., NCB, Rm. 10103, Philadelphia, PA 19102-1192. Tel.: 215-762-7195; Fax: 215-762-4452; E-mail: amazin{at}drexelmed.edu.


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This article has been cited by other articles:


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Proc. Natl. Acad. Sci. USAHome page
O. M. Mazina and A. V. Mazin
Human Rad54 protein stimulates human Mus81-Eme1 endonuclease
PNAS, November 25, 2008; 105(47): 18249 - 18254.
[Abstract] [Full Text] [PDF]




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