期刊
CURRENT GENETICS
卷 54, 期 4, 页码 197-211出版社
SPRINGER
DOI: 10.1007/s00294-008-0212-z
关键词
DNA repair; recombination; UV tolerance; S. pombe
资金
- Swiss National Science Foundation
- Swiss SCOPES [7SUPJ062355, IB73AO-110965]
- Howard Hughes Medical Institute [55000299]
- Russian Fund for Basic Research [06-04-48470]
DNA double-strand break (DSB) repair mediated by the Rad51 pathway of homologous recombination is conserved in eukaryotes. In yeast, Rad51 paralogs, Saccharomyces cerevisiae Rad55-Rad57 and Schizosaccharomyces pombe Rhp55-Rhp57, are mediators of Rad51 nucleoprotein formation. The recently discovered S. pombe Sfr1/Dds20 protein has been shown to interact with Rad51 and to operate in the Rad51-dependent DSB repair pathway in parallel to the paralog-mediated pathway. Here we show that Sfr1 is a nuclear protein and acts downstream of Rad50 in DSB processing. sfr1 Delta is epistatic to rad18(-) stop and rad60(-), and Sfr1 is a high-copy suppressor of the replication and repair defects of a rad60 mutant. Sfr1 functions in a Cds1-independent UV damage tolerance mechanism. In contrast to mitotic recombination, meiotic recombination is significantly reduced in sfr1 Delta strains. Our data indicate that Sfr1 acts in DSB repair mainly outside of S-phase, and is required for wild-type levels of meiotic recombination. We suggest that Sfr1 acts early in recombination and has a specific role in Rad51 filament assembly, distinct from that of the Rad51 paralogs.
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