| Literature DB >> 17304215 |
Yufuko Akamatsu1, Yasuhiro Tsutsui, Takashi Morishita, Md Shahjahan P Siddique, Yumiko Kurokawa, Mitsunori Ikeguchi, Fumiaki Yamao, Benoit Arcangioli, Hiroshi Iwasaki.
Abstract
Several accessory proteins referred to as mediators are required for the full activity of the Rad51 (Rhp51 in fission yeast) recombinase. In this study, we analyzed in vivo functions of the recently discovered Swi5/Sfr1 complex from fission yeast. In normally growing cells, the Swi5-GFP protein localizes to the nucleus, where it forms a diffuse nuclear staining pattern with a few distinct foci. These spontaneous foci do not form in swi2Delta mutants. Upon UV irradiation, Swi5 focus formation is induced in swi2Delta mutants, a response that depends on Sfr1 function, and Sfr1 also forms foci that colocalize with damage-induced Rhp51 foci. The number of UV-induced Rhp51 foci is partially reduced in swi5Delta and rhp57Delta mutants and completely abolished in an swi5Delta rhp57Delta double mutant. An assay for products generated by HO endonuclease-induced DNA double-strand breaks (DSBs) reveals that Rhp51 and Rhp57, but not Swi5/Sfr1, are essential for crossover production. These results suggest that Swi5/Sfr1 functions as an Rhp51 mediator but processes DSBs in a manner different from that of the Rhp55/57 mediator.Entities:
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Year: 2007 PMID： 17304215 PMCID： PMC1817630 DOI： 10.1038/sj.emboj.7601582
Source DB: PubMed Journal: EMBO J ISSN： 0261-4189 Impact factor: 11.598