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Nucleic Acids Research 2006 34(9):2833-2843; doi:10.1093/nar/gkl366
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Published online 22 May 2006

© The Author 2006. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions@oxfordjournals.org

Article

Disparate requirements for the Walker A and B ATPase motifs of human RAD51D in homologous recombination

Claudia Wiese*, John M. Hinz1, Robert S. Tebbs1, Peter B. Nham1, Salustra S. Urbin1, David W. Collins, Larry H. Thompson1 and David Schild

Life Sciences Division, Lawrence Berkeley National Laboratory Berkeley, CA 94720, USA 1 Biosciences Directorate, Lawrence Livermore National Laboratory P.O. Box 808, Livermore, CA 94551, USA

*To whom correspondence should be addressed. Tel: +1 510 486 4024; Fax: +1 510 486 6816; Email: cwiese{at}lbl.gov

Received April 18, 2006. Accepted April 26, 2006.

In vertebrates, homologous recombinational repair (HRR) requires RAD51 and five RAD51 paralogs (XRCC2, XRCC3, RAD51B, RAD51C and RAD51D) that all contain conserved Walker A and B ATPase motifs. In human RAD51D we examined the requirement for these motifs in interactions with XRCC2 and RAD51C, and for survival of cells in response to DNA interstrand crosslinks (ICLs). Ectopic expression of wild-type human RAD51D or mutants having a non-functional A or B motif was used to test for complementation of a rad51d knockout hamster CHO cell line. Although A-motif mutants complement very efficiently, B-motif mutants do not. Consistent with these results, experiments using the yeast two- and three-hybrid systems show that the interactions between RAD51D and its XRCC2 and RAD51C partners also require a functional RAD51D B motif, but not motif A. Similarly, hamster Xrcc2 is unable to bind to the non-complementing human RAD51D B-motif mutants in co-immunoprecipitation assays. We conclude that a functional Walker B motif, but not A motif, is necessary for RAD51D's interactions with other paralogs and for efficient HRR. We present a model in which ATPase sites are formed in a bipartite manner between RAD51D and other RAD51 paralogs.


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