Abstract
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.
Original language | English (US) |
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Pages (from-to) | 3799-3802 |
Number of pages | 4 |
Journal | Journal of Biological Chemistry |
Volume | 273 |
Issue number | 7 |
DOIs | |
State | Published - Feb 13 1998 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology