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Originally published In Press as doi:10.1074/jbc.M105719200 on February 7, 2002

J. Biol. Chem., Vol. 277, Issue 16, 14315-14320, April 19, 2002
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Homologous Pairing and Ring and Filament Structure Formation Activities of the Human Xrcc2·Rad51D Complex*

Hitoshi KurumizakaDagger §, Shukuko Ikawa||, Maki NakadaDagger , Rima EnomotoDagger , Wataru KagawaDagger **, Takashi KinebuchiDagger , Mitsuyoshi YamazoeDagger Dagger , Shigeyuki YokoyamaDagger §**§§, and Takehiko Shibata||§§

From the Dagger  RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan, the § Cellular Signaling Laboratory, RIKEN Harima Institute at SPring-8, 1-1-1 Kohto, Mikazuki-cho, Sayo, Hyogo 679-5143, Japan, the || Cellular and Molecular Biology Laboratory, RIKEN, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan,  Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Corporation, 1637 Yana, Kisarazu, Chiba 292-0812, Japan, the ** Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan, and Dagger Dagger  Faculty of Medicine, Kyoto University, Konoe Yoshida, Sakyo-ku, Kyoto 606-8501, Japan

The Xrcc2 and Rad51D/Rad51L3 proteins, which belong to the Rad51 paralogs, are required for homologous recombinational repair (HRR) in vertebrates. The Xrcc2 and Rad51D/Rad51L3 genes, whose products interact with each other, have essential roles in ensuring normal embryonic development. In the present study, we coexpressed the human Xrcc2 and Rad51D/Rad51L3 proteins (Xrcc2 and Rad51D, respectively) in Escher- ichia coli, and purified the Xrcc2·Rad51D complex to homogeneity. The Xrcc2·Rad51D complex catalyzed homologous pairing between single-stranded and double-stranded DNA, similar to the function of the Xrcc3· Rad51C complex, which is another complex of the Rad51 paralogs. An electron microscopic analysis showed that Xrcc2·Rad51D formed a multimeric ring structure in the absence of DNA. In the presence of ssDNA, Xrcc2·Rad51D formed a filamentous structure, which is commonly observed among the human homologous pairing proteins, Rad51, Rad52, and Xrcc3·Rad51C.

* This work was supported in part by the Bioarchitect Research Program (RIKEN), Core Research for Evolutional Science and Technology (CREST) of Japan Science and Technology Corporation (JST), and a grant-in-aid from the Ministry of Education, Sports, Culture, Science, and Technology, Japan.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.

§§ To whom correspondence may be addressed. E-mail: yokoyama@biochem.s.u-tokyo.ac.jp or tshibata@postman.riken.go.jp.

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


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