Letter abstract
Nature Cell Biology 8, 1284 - 1290 (2006)
Published online: 1 October 2006 | doi:10.1038/ncb1488
Control of Rad52 recombination activity by double-strand break-induced SUMO modification
Meik Sacher1, Boris Pfander1,2, Carsten Hoege1,3 & Stefan Jentsch1
Homologous recombination is essential for genetic exchange, meiosis and error-free repair of double-strand breaks1. Central to this process is Rad52, a conserved homo-oligomeric ring-shaped protein, which mediates the exchange of the early recombination factor RPA by Rad51 and promotes strand annealing2, 3. Here, we report that Rad52 of Saccharomyces cerevisiae is modified by the ubiquitin-like protein SUMO, primarily at two sites that flank the conserved Rad52 domain. Sumoylation is induced on DNA damage and triggered by Mre11–Rad50–Xrs2 (MRX) complex-governed double-strand breaks (DSBs). Although sumoylation-defective Rad52 is largely recombination proficient, mutant analysis revealed that the SUMO modification sustains Rad52 activity and concomitantly shelters the protein from accelerated proteasomal degradation. Furthermore, our data indicate that sumoylation becomes particularly relevant for those Rad52 molecules that are engaged in recombination.
- Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
- Present address: Cancer Research UK, Clare Hall Laboratories, Blanche Lane, South Mimms, EN6 3LD, UK.
- Present address: Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01307 Dresden, Germany.
Correspondence to: Stefan Jentsch1 e-mail: Jentsch@biochem.mpg.de
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