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Originally published In Press as doi:10.1074/jbc.M108306200 on December 13, 2001

J. Biol. Chem., Vol. 277, Issue 10, 8406-8411, March 8, 2002
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RAD51C Interacts with RAD51B and Is Central to a Larger Protein Complex in Vivo Exclusive of RAD51*

Kristi A. MillerDagger , Daniel M. YoshikawaDagger , Ian R. McConnellDagger , Robin ClarkDagger , David Schild§, and Joanna S. AlbalaDagger ||

From the Dagger  Lawrence Livermore National Laboratory, Livermore, California 94550 and the § Lawrence Berkeley National Laboratory, Berkeley, California 94720

RAD51B and RAD51C are two of five known paralogs of the human RAD51 protein that are thought to function in both homologous recombination and DNA double-strand break repair. This work describes the in vitro and in vivo identification of the RAD51B/RAD51C heterocomplex. The RAD51B/RAD51C heterocomplex was isolated and purified by immunoaffinity chromatography from insect cells co-expressing the recombinant proteins. Moreover, co-immunoprecipitation of the RAD51B and RAD51C proteins from HeLa, MCF10A, and MCF7 cells strongly suggests the existence of an endogenous RAD51B/RAD51C heterocomplex. We extended these observations to examine the interaction between the RAD51B/RAD51C complex and the other RAD51 paralogs. Immunoprecipitation using protein-specific antibodies showed that RAD51C is central to a single large protein complex and/or several smaller complexes with RAD51B, RAD51D, XRCC2, and XRCC3. However, our experiments showed no evidence for the inclusion of RAD51 within these complexes. Further analysis is required to elucidate the function of the RAD51B/RAD51C heterocomplex and its association with the other RAD51 paralogs in the processes of homologous recombination and DNA double-strand break repair.

* This work was supported by Grant CA81019-01 from the National Cancer Institute and Grant 5KB-0123 from the California Breast Cancer Research Program (to J. S. A.). This work was performed under the auspices of the United States Department of Energy by the University of California, Lawrence Livermore National Laboratory under Contract No. W-7405-ENG-48.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.

Supported by National Institutes of Health Grant GM30990, administered under DOE Contract No. DE-AC03-76SF00098 to Lawrence Berkeley National Laboratory.

|| To whom correspondence should be addressed: Biology and Biotechnology Research Program, Lawrence Livermore National Laboratory, 7000 East Ave., L-448, Livermore, CA 94550. Tel.: 925-422-6442; Fax: 925-424-6605; E-mail: albala1@llnl.gov.

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


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