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Sws1 is a conserved regulator of homologous recombination in eukaryotic cells
Author(s) -
Martín Victoria,
Chahwan Charly,
Gao Hui,
Blais Véronique,
Wohlschlegel James,
Yates John R,
McGowan Clare H,
Russell Paul
Publication year - 2006
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7601141
Subject(s) - library science , biology , computer science
Rad52‐dependent homologous recombination (HR) is regulated by the antirecombinase activities of Srs2 and Rqh1/Sgs1 DNA helicases in fission yeast and budding yeast. Functional analysis of Srs2 in Schizosaccharomyces pombe led us to the discovery of Sws1, a novel HR protein with a SWIM‐type Zn finger. Inactivation of Sws1 suppresses the genotoxic sensitivity of srs2 Δ and rqh1 Δ mutants and rescues the inviability of srs2 Δ rqh1 Δ cells. Sws1 functions at an early step of recombination in a pro‐recombinogenic complex with Rlp1 and Rdl1, two RecA‐like proteins that are most closely related to the human Rad51 paralogs XRCC2 and RAD51D, respectively. This finding indicates that the XRCC2–RAD51D complex is conserved in lower eukaryotes. A SWS1 homolog exists in human cells. It associates with RAD51D and ablating its expression reduces the number of RAD51 foci. These studies unveil a conserved pathway for the initiation and control of HR in eukaryotic cells.