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- W3118998329 abstract "Homologous recombination (HR) is essential for maintenance of genome integrity. Rad51 paralogs fulfill a conserved but undefined role in HR, and their mutations are associated with increased cancer risk in humans. Here, we use single-molecule imaging to reveal that the Saccharomyces cerevisiae Rad51 paralog complex Rad55-Rad57 promotes assembly of Rad51 recombinase filament through transient interactions, providing evidence that it acts like a classical molecular chaperone. Srs2 is an ATP-dependent anti-recombinase that downregulates HR by actively dismantling Rad51 filaments. Contrary to the current model, we find that Rad55-Rad57 does not physically block the movement of Srs2. Instead, Rad55-Rad57 promotes rapid re-assembly of Rad51 filaments after their disruption by Srs2. Our findings support a model in which Rad51 is in flux between free and single-stranded DNA (ssDNA)-bound states, the rate of which is controlled dynamically though the opposing actions of Rad55-Rad57 and Srs2." @default.
- W3118998329 created "2021-01-18" @default.
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- W3118998329 date "2021-03-01" @default.
- W3118998329 modified "2023-10-17" @default.
- W3118998329 title "The Rad51 paralog complex Rad55-Rad57 acts as a molecular chaperone during homologous recombination" @default.
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- W3118998329 doi "https://doi.org/10.1016/j.molcel.2020.12.019" @default.
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