bioRxiv Biochemistry
bioRxiv Biochemistry
5 years ago

Structure of Zip2:Spo16, a conserved XPF:ERCC1-like complex critical for meiotic crossover formation

K. D., K., Arora, Corbett
In eukaryotic meiosis, generation of haploid gametes depends on the formation of inter-homolog crossovers, which enable homolog segregation to reduce ploidy 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 to form a complex critical for crossover formation and control. We reconstituted and determined the crystal structure of a Zip2:Spo16 subcomplex, revealing a heterodimer structurally related to the XPF:ERCC1 endonuclease complex. We show that Zip2:Spo16 binds specific DNA structures found in early meiotic recombination intermediates, but does not possess and intact endonuclease site. Overall, our data support a model in which Zip2:Spo16 binds and stabilizes early meiotic recombination intermediates, while the associated TPR protein Zip4 recruits additional factors to promote crossover formation and license synaptonemal complex assembly. Given the recent identification of Zip2 homologs outside fungi, the molecular mechanisms we outline are likely conserved throughout eukaryotes.

Publisher URL: http://biorxiv.org/cgi/content/short/258194v1

DOI: 10.1101/258194

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