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J Biol Chem, Vol. 273, Issue 7, 3799-3802, February 13, 1998

COMMUNICATION
Regulation of Rad51 Function by c-Abl in Response to DNA Damage

Zhi-Min Yuan, Yinyin Huang, Takatoshi Ishiko, Shuji Nakada, Taiju Utsugisawa, Surender Kharbanda, Rong Wang, Patrick Sung^§, Akira Shinohara^¶, Ralph Weichselbaum, and Donald Kufe

From the Division of Cancer Pharmacology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115, the  Mass Spectroscopy Center, The Rockefeller University, New York, New York 10021, the ^§ Institute of Biotechnology and Center for Molecular Medicine, University of Texas Health Science Center at San Antonio, San Antonio, Texas 78245-3207, the ^¶ Department of Biology, Faculty of Science, Osaka University, Osaka 560, Japan, and the  Department of Radiation and Cellular Oncology, University of Chicago, Chicago, Illinois 60637

The Rad51 protein, a homolog of bacterial RecA, functions in DNA double-strand break repair and genetic recombination. Whereas Rad51 catalyzes ATP-dependent pairing and strand exchange between homologous DNA molecules, regulation of this function is unknown. The c-Abl tyrosine kinase is activated by ionizing radiation and certain other DNA-damaging agents. Here we demonstrate that c-Abl interacts constitutively with Rad51. We show that c-Abl phosphorylates Rad51 on Tyr-54 in vitro. The results also show that treatment of cells with ionizing radiation induces c-Abl-dependent phosphorylation of Rad51. Phosphorylation of Rad51 by c-Abl inhibits the binding of Rad51 to DNA and the function of Rad51 in ATP-dependent DNA strand exchange reactions. These findings represent the first demonstration that Rad51 is regulated by phosphorylation and support a functional role for c-Abl in regulating Rad51-dependent recombination in the response to DNA damage.

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