Proceedings of the National Academy of Sciences · 2018 · 39 citations · 49 references
Life SciencesGeneticsMolecular BiologyCell DivisionGametogenesisRecombinationCrossing OverHomologous RecombinationMeiosis In Germ CellsMeiotic RecombinationRecombination IntermediatesRecombination ProteinsDmc1 ProteinDmc1 RecombinaseDmc1 RegulationHomologous Recombination IntermediatesMeiotic Recombination ControlMeiotic Recombination IntermediatesMeiotic Recombination PathwaysMeiotic Recombination Proteins
, the Superfamily 1 (Sf1) helicase Srs2, which is an ATP hydrolysis-dependent motor protein that actively dismantles recombination intermediates, promotes synthesis-dependent strand annealing, the result of which is a reduction in cross-over recombination products. Here, we show that the meiosis-specific recombinase Dmc1 is a potent inhibitor of Srs2. Biochemical and single-molecule assays demonstrate that Dmc1 acts by inhibiting Srs2 ATP hydrolysis activity, which prevents the motor protein from undergoing ATP hydrolysis-dependent translocation on Dmc1-bound recombination intermediates. We propose a model in which Dmc1 helps contribute to cross-over formation during meiosis by antagonizing the antirecombinase activity of Srs2.
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