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Originally published In Press as doi:10.1074/jbc.M206511200 on August 8, 2002

J. Biol. Chem., Vol. 277, Issue 42, 40132-40141, October 18, 2002
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Interaction with Rad51 Is Indispensable for Recombination Mediator Function of Rad52*

Lumir KrejciDagger , Binwei Song§, Wendy Bussen, Rodney Rothstein, Uffe H. MortensenDagger ||**, and Patrick Sung

From the Department of Molecular Medicine/Institute of Biotechnology, University of Texas Health Science Center at San Antonio, San Antonio, Texas 78245-3207, the  Department of Genetics and Development, Columbia University College of Physician and Surgeons, New York, New York 10032-2704, and || BioCentrum-DTU, Technical University of Denmark, 2800 Lyngby, Denmark

In the yeast Saccharomyces cerevisiae, the RAD52 gene is indispensable for homologous recombination and DNA repair. Rad52 protein binds DNA, anneals complementary ssDNA strands, and self-associates to form multimeric complexes. Moreover, Rad52 physically interacts with the Rad51 recombinase and serves as a mediator in the Rad51-catalyzed DNA strand exchange reaction. Here, we examine the functional significance of the Rad51/Rad52 interaction. Through a series of deletions, we have identified residues 409-420 of Rad52 as being indispensable and likely sufficient for its interaction with Rad51. We have constructed a four-amino acid deletion mutation within this region of Rad52 to ablate its interaction with Rad51. We show that the rad52Delta 409-412 mutant protein is defective in the mediator function in vitro even though none of the other Rad52 activities, namely, DNA binding, ssDNA annealing, and protein oligomerization, are affected. We also show that the sensitivity of the rad52Delta 409-412 mutant to ionizing radiation can be complemented by overexpression of Rad51. These results thus demonstrate the significance of the Rad51-Rad52 interaction in homologous recombination.

* This work was supported by United States Public Health Service Grants RO1 ES07061, RO1 GM57814, RO1 GM50237, and T32 CA86800, by Human Frontier Research Project Grant HFSP RG0178/2000-M, and by The Danish Technical Research Council, by the Alfred Benzon Foundation, and by NATO Science Fellowship.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.

Dagger To whom correspondence may be addressed. Tel.: 210-567-7215; Fax: 210-567-7277; E-mail: krejci@uthscsa.edu.

§ Present address: Dept. of Biochemistry, Emory University School of Medicine, 1510 Clifton Rd., Atlanta, GA 30322.

** To whom correspondence may also be addressed. Tel.: 45-4525-2701; Fax: 45-4588-4148; E-mail: um@buiocentrum.dtu.dk.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.


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