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Originally published In Press as doi:10.1074/jbc.M001473200 on April 3, 2000

J. Biol. Chem., Vol. 275, Issue 22, 16443-16449, June 2, 2000
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Evidence for Simultaneous Protein Interactions between Human Rad51 Paralogs*

David SchildDagger , Yi-ching Lio, David W. Collins, Tswakai Tsomondo§, and David J. Chen

From the Life Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720

In yeast, the Rad51-related proteins include Rad55 and Rad57, which form a heterodimer that interacts with Rad51. Five human Rad51 paralogs have been identified (XRCC2, XRCC3, Rad51B/Rad51L1, Rad51C/Rad51L2, and Rad51D/Rad51L3), and each interacts with one or more of the others. Previously we reported that HsRad51 interacts with XRCC3, and Rad51C interacts with XRCC3, Rad51B, and HsRad51. Here we report that in the yeast two-hybrid system, Rad51D interacts with XRCC2 and Rad51C. No other interactions, including self-interactions, were found, indicating that the observed interactions are specific. The yeast Rad51 interacts with human Rad51 and XRCC3, suggesting Rad51 conservation since the human yeast divergence. Data from yeast three-hybrid experiments indicate that a number of the pairs of interactions between human Rad51 paralogs can occur simultaneously. For example, Rad51B expression enhances the binding of Rad51C to XRCC3 and to HsRad51D, and Rad51C expression allows the indirect interaction of Rad51B with Rad51D. Experiments using 6xHis-tagged proteins in the baculovirus system confirm several of our yeast results, including Rad51B interaction with Rad51D only when Rad51C is simultaneously expressed and Rad51C interaction with XRCC2 only when Rad51D is present. These results suggest that these proteins may participate in one complex or multiple smaller ones.

* This work was supported by National Institutes of Health Grants GM30990 (to D. S.) and CA74046 (to D. J. C.) and by a United States Department of Energy grant (to D. J. C.).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 should be addressed: Life Sciences Div., Lawrence Berkeley Natl. Laboratory, Mail Stop 70A-1118, 1 Cyclotron Rd., Berkeley, CA 94720. Tel.: 510-486-6013 or 510-486-4024; Fax: 510-486-4475; E-mail: dschild@lbl.gov.

§ Supported by a supplement to National Institutes of Health Grant GM30990 for the support of minority undergraduates. Present address: Dept. of Ecology and Evolutionary Biology, Cornell University, Ithaca, NY 14853.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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