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A more recent version of this article appeared on April 12, 2002
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M105719200v1
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Papers In Press, published online ahead of print February 7, 2002
J. Biol. Chem, 10.1074/jbc.M105719200
Submitted on June 20, 2001
Revised on January 11, 2002
Accepted on February 6, 2002

Homologous-pairing, and ring- and filament-structure formation activities of the human Xrcc2-Rad51D complex

Hitoshi Kurumizaka, Shukuko Ikawa, Maki Nakada, Rima Enomoto, Wataru Kagawa, Takashi Kinebuchi, Mitsuyoshi Yamazoe, Shigeyuki Yokoyama, and Takehiko Shibata

Cellular & Molecular Biology Laboratory, RIKEN, Wako-shi, Saitama 351-0198

Corresponding Author: tshibata{at}postman.riken.go.jp

The Xrcc2 and Rad51D/Rad51L3 proteins, which belong to the Rad51 paralogs, are required for homologous recombination 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 Escherichia coli, and purified the Xrcc2-Rad51D complex to homogeneity. The Xrcc2-Rad51D complex catalyzed homologous pairing between single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA), 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.


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