The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments

Xavier Veaute (), Josette Jeusset, Christine Soustelle, Stephen C. Kowalczykowski, Eric Le Cam and Francis Fabre ()
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Xavier Veaute: UMR217 CNRS/CEA
Josette Jeusset: UMR 81126 CNRS/IGR/UPS, Institut Gustave Roussy
Christine Soustelle: UMR217 CNRS/CEA
Stephen C. Kowalczykowski: University of California
Eric Le Cam: UMR 81126 CNRS/IGR/UPS, Institut Gustave Roussy
Francis Fabre: UMR217 CNRS/CEA

Nature, 2003, vol. 423, issue 6937, 309-312

Abstract: Abstract Homologous recombination is a ubiquitous process with key functions in meiotic and vegetative cells for the repair of DNA breaks. It is initiated by the formation of single-stranded DNA on which recombination proteins bind to form a nucleoprotein filament that is active in searching for homology, in the formation of joint molecules and in the exchange of DNA strands1. This process contributes to genome stability but it is also potentially dangerous to cells if intermediates are formed that cannot be processed normally and thus are toxic or generate genomic rearrangements. Cells must therefore have developed strategies to survey recombination and to prevent the occurrence of such deleterious events. In Saccharomyces cerevisiae, genetic data have shown that the Srs2 helicase negatively modulates recombination2,3, and later experiments suggested that it reverses intermediate recombination structures4,5,6,7. Here we show that DNA strand exchange mediated in vitro by Rad51 is inhibited by Srs2, and that Srs2 disrupts Rad51 filaments formed on single-stranded DNA. These data provide an explanation for the anti-recombinogenic role of Srs2 in vivo and highlight a previously unknown mechanism for recombination control.

Date: 2003
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DOI: 10.1038/nature01585

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