SRS2 is required for MUS81-dependent CO formation in zmm mutants.

Helicases are enzymes that use the energy derived from ATP hydrolysis to translocate along and unwind nucleic acids. Accordingly, helicases are instrumental in maintaining genomic integrity and ensuring genetic diversity. Srs2 is a multi-functional DNA helicase that dismantles Rad51 nucleofilaments...

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Bibliographic Details
Main Authors: Valentine Petiot, Floriane Chéron, Charles I White, Olivier Da Ines
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2025-08-01
Series:PLoS Genetics
Online Access:https://doi.org/10.1371/journal.pgen.1011637
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Summary:Helicases are enzymes that use the energy derived from ATP hydrolysis to translocate along and unwind nucleic acids. Accordingly, helicases are instrumental in maintaining genomic integrity and ensuring genetic diversity. Srs2 is a multi-functional DNA helicase that dismantles Rad51 nucleofilaments and regulates DNA strand invasion to prevent excessive or inappropriate homologous recombination in yeast. Consistently, the deletion of Srs2 has significant consequences for the maintenance of genome integrity in mitotic cells. In contrast, its role in meiotic recombination remains less clear. We present here substantial evidence that SRS2 plays an important role in meiotic recombination in the model plant Arabidopsis thaliana. Arabidopsis srs2 mutants exhibit moderate defects in DNA damage-induced RAD51 focus formation, but SRS2 is dispensable for DNA repair and RAD51-dependent recombination in somatic cells. Meiotic progression and fertility appear unaffected in srs2 plants but, strikingly, the absence of SRS2 leads to increased genetic interference accompanied by increased numbers of Class I COs and a reduction in MUS81-dependent Class II COs. We propose that SRS2 plays a role in MUS81-mediated resolution of a subset of recombination intermediates into Class II CO. The absence of SRS2 would thus lead to the alternative channeling of these recombination intermediates into the Class I CO pathway, resulting in an increased proportion of Class I CO.
ISSN:1553-7390
1553-7404