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- W2002748750 endingPage "347" @default.
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- W2002748750 abstract "At the final step of homologous recombination, Holliday junction-containing joint molecules (JMs) are resolved to form crossover or noncrossover products. The enzymes responsible for JM resolution in vivo remain uncertain, but three distinct endonucleases capable of resolving JMs in vitro have been identified: Mus81-Mms4(EME1), Slx1-Slx4(BTBD12), and Yen1(GEN1). Using physical monitoring of recombination during budding yeast meiosis, we show that all three endonucleases are capable of promoting JM resolution in vivo. However, in mms4 slx4 yen1 triple mutants, JM resolution and crossing over occur efficiently. Paradoxically, crossing over in this background is strongly dependent on the Blooms helicase ortholog Sgs1, a component of a well-characterized anticrossover activity. Sgs1-dependent crossing over, but not JM resolution per se, also requires XPG family nuclease Exo1 and the MutLγ complex Mlh1-Mlh3. Thus, Sgs1, Exo1, and MutLγ together define a previously undescribed meiotic JM resolution pathway that produces the majority of crossovers in budding yeast and, by inference, in mammals." @default.
- W2002748750 created "2016-06-24" @default.
- W2002748750 creator A5011827924 @default.
- W2002748750 creator A5024023733 @default.
- W2002748750 creator A5043745359 @default.
- W2002748750 creator A5045413691 @default.
- W2002748750 date "2012-04-01" @default.
- W2002748750 modified "2023-10-08" @default.
- W2002748750 title "Delineation of Joint Molecule Resolution Pathways in Meiosis Identifies a Crossover-Specific Resolvase" @default.
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- W2002748750 doi "https://doi.org/10.1016/j.cell.2012.03.023" @default.
- W2002748750 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3377385" @default.
- W2002748750 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22500800" @default.
- W2002748750 hasPublicationYear "2012" @default.