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- W3200477716 abstract "Abstract In eukaryotic meiosis, generation of haploid gametes depends on the formation of inter-homolog crossovers, which enable the pairing, physical linkage, and eventual segregation of homologs in the meiosis I division. A class of conserved meiosis-specific proteins, collectively termed ZMMs, are required for formation and spatial control of crossovers throughout eukaryotes. Here, we show that three S. cerevisiae ZMM proteins – Zip2, Zip4, and Spo16 – interact with one another and form a DNA-binding complex critical for crossover formation and control. We determined the crystal structure of a Zip2:Spo16 subcomplex, revealing a heterodimer structurally related to the XPF:ERCC1 endonuclease complex. Zip2:Spo16 lacks an endonuclease active site, but binds specific DNA structures found in early meiotic recombination intermediates. Mutations in multiple DNA-binding surfaces on the Zip2:Spo16 complex severely compromise DNA binding, supporting a model in which the complex’s central and HhH domains cooperate to bind DNA. Overall, our data support a model in which the Zip2:Zip4:Spo16 complex binds and stabilizes early meiotic recombination intermediates, then coordinates additional factors to promote crossover formation and license downstream events including synaptonemal complex assembly." @default.
- W3200477716 created "2021-09-27" @default.
- W3200477716 creator A5087136833 @default.
- W3200477716 creator A5090773705 @default.
- W3200477716 date "2018-02-01" @default.
- W3200477716 modified "2023-10-13" @default.
- W3200477716 title "Structure of Zip2:Spo16, a conserved XPF:ERCC1-like complex critical for meiotic crossover formation" @default.
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- W3200477716 doi "https://doi.org/10.1101/258194" @default.
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