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Molecular and Cellular Biology, September 2000, p. 6476-6482, Vol. 20, No. 17
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

The Rad51 Paralog Rad51B Promotes Homologous Recombinational Repair

Minoru Takata,1,2 Masao S. Sasaki,3 Eiichiro Sonoda,4 Toru Fukushima,1 Ciaran Morrison,1 Joanna S. Albala,5 Sigrid M. A. Swagemakers,4 Roland Kanaar,4 Larry H. Thompson,5 and Shunichi Takeda1,2,*

Bayer-Chair Department of Molecular Immunology and Allergy, Faculty of Medicine,1 CREST, JST (Japan Science and Technology),2 and Radiation Biology Center,3 Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan; Medical Genetics Center, Department of Cell Biology and Genetics, Erasmus University Rotterdam, 3000 DR Rotterdam, The Netherlands4; and Biology and Biotechnology Research Program, Lawrence Livermore National Laboratory, Livermore, California 94551-08085

Received 9 September 1999/Returned for modification 27 October 1999/Accepted 26 January 2000

The highly conserved Saccharomyces cerevisiae Rad51 protein plays a central role in both mitotic and meiotic homologous DNA recombination. Seven members of the Rad51 family have been identified in vertebrate cells, including Rad51, Dmc1, and five Rad51-related proteins referred to as Rad51 paralogs, which share 20 to 30% sequence identity with Rad51. In chicken B lymphocyte DT40 cells, we generated a mutant with RAD51B/RAD51L1, a member of the Rad51 family, knocked out. RAD51B-/- cells are viable, although spontaneous chromosomal aberrations kill about 20% of the cells in each cell cycle. Rad51B deficiency impairs homologous recombinational repair (HRR), as measured by targeted integration, sister chromatid exchange, and intragenic recombination at the immunoglobulin locus. RAD51B-/- cells are quite sensitive to the cross-linking agents cisplatin and mitomycin C and mildly sensitive to gamma -rays. The formation of damage-induced Rad51 nuclear foci is much reduced in RAD51B-/- cells, suggesting that Rad51B promotes the assembly of Rad51 nucleoprotein filaments during HRR. These findings show that Rad51B is important for repairing various types of DNA lesions and maintaining chromosome integrity.

* Corresponding author. Present address: CREST Research Project, Radiation Genetics, Faculty of Medicine, Kyoto University, Konoe Yoshida, Sakyo-ku, Kyoto 606-8501, Japan. Phone: 81-75-753-4410. Fax: 81-75-753-4419. E-mail: stakeda{at}rg1.rg.med.kyoto-u.ac.jp.

Molecular and Cellular Biology, September 2000, p. 6476-6482, Vol. 20, No. 17
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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