DNA helicase Srs2 disrupts the Rad51 presynaptic filament

By L. Krejci, S. V. Komen, Ying Li, J. Villemain, Mothe Sreedhar Reddy, H. Klein, T. Ellenberger, P. Sung. Nature, 2003

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Surviving the breakup: the DNA damage checkpoint. (2006, background): “Biochemical analysis of the Srs2 helicase shows that it can remove Rad51 from ssDNA in vitro, and deletion of Rad51 substantially alleviates srs2 ’s recovery defect (Figure 3a, b) (71, 150, 151).”
Recombination proteins in yeast. (2004, background): “In vitro, the Srs2 protein inhibits strand exchange mediated by Rad51 (101, 221).”
Homologous recombination and its regulation (2012, background): “Direct evidence for an anti-Rad51 function came from biochemical studies showing that catalytic amounts of Srs2 efficiently dismantle Rad51 presynaptic filaments (76,77) (Figure 2).”
Regulation of homologous recombination in eukaryotes (2010, background): “Unlike yeast Srs2, RTEL1 cannot dissociate RAD51 from ssDNA (11, 90, 158).”
Biochemical properties of Hmi1p, a DNA helicase from Saccharomyces cerevisiae mitochondria (2006, background): “Srs2p was recently shown to negatively control the recombination by dismantling Rad51p filaments formed on ssDNA, which are required for initiation of the recombination process (Krejci et al., 2003; Veaute et al., 2003).”
Repair Pathway Choices and Consequences at the Double-Strand Break (2015, neutral): “For example, the budding yeast Srs2 helicase disrupts the Rad51–ssDNA presynaptic nucleofilament in vitro, and has been implicated in the prevention of undesirable HR [46,77] and promotion of efficient alt-EJ [50].”