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Published online 11 May 2004

Nucleic Acids Research, 2004, Vol. 32, No. 8 2556-2565
© 2004 Oxford University Press

Preferential binding to branched DNA strands and strand-annealing activity of the human Rad51B, Rad51C, Rad51D and Xrcc2 protein complex

Hiroshi Yokoyama1,2, Naoyuki Sarai1,2, Wataru Kagawa1, Rima Enomoto1, Takehiko Shibata3,4, Hitoshi Kurumizaka*,1,4,5 and Shigeyuki Yokoyama1,2,6

1 RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan, 2 Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan, 3 Cellular and Molecular Biology Laboratory, RIKEN, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan, 4 Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Corporation, 1637 Yana, Kisarazu, Chiba 292-0812, Japan, 5 Waseda University School of Science and Engineering, 3-4-1 Okubo, Shinjuku-ku, Tokyo 169-8555, Japan and 6 RIKEN Harima Institute at Spring-8, 1-1-1 Kohto, Mikazuki-cho, Sayo, Hyogo 679-5148, Japan

*To whom correspondence should be addressed. Tel: + 81 3 5286 8189; Fax: + 81 3 5292 9211; Email: kurumizaka{at}waseda.jp
Correspondence may also be addressed to Shigeyuki Yokoyama. Tel: +81 45 503 9196; Fax: +81 45 503 9195; Email: yokoyama{at}biochem.s.u-tokyo.ac.jp
Present address:
Hiroshi Yokoyama, National Agriculture and Bio-oriental Research Organization, National Institute of Livestock and Grassland Science, 2 Ikenodai, Tsukuba, Ibaraki 305-0901, Japan
The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors

Received March 8, 2004; Revised and Accepted April 12, 2004

The Rad51B, Rad51C, Rad51D and Xrcc2 proteins are Rad51 paralogs, and form a complex (BCDX2 complex) in mammalian cells. Mutant cells defective in any one of the Rad51-paralog genes exhibit spontaneous genomic instability and extreme sensitivity to DNA-damaging agents, due to inefficient recombinational repair. Therefore, the Rad51 paralogs play important roles in the maintenance of genomic integrity through recombinational repair. In the present study, we examined the DNA-binding preference of the human BCDX2 complex. Competitive DNA-binding assays using seven types of DNA substrates, single-stranded DNA (ssDNA), double-stranded DNA, 5'- and 3'-tailed duplexes, nicked duplex DNA, Y-shaped DNA and a synthetic Holliday junction, revealed that the BCDX2 complex preferentially bound to the two DNA substrates with branched structures (the Y-shaped DNA and the synthetic Holliday junction). Furthermore, the BCDX2 complex catalyzed the strand-annealing reaction between a long linear ssDNA (1.2 kb in length) and its complementary circular ssDNA. These properties of the BCDX2 complex may be important for its roles in the maintenance of chromosomal integrity.


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