Open AccessPCH-2 collaborates with CMT-1 to proofread meiotic homolog interactions
Author(s) -
Stefani Giacopazzi,
Daniel Vong,
Alice Devigne,
Needhi Bhalla
Publication year - 2020
Publication title -
plos genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.587
H-Index - 233
eISSN - 1553-7404
pISSN - 1553-7390
DOI - 10.1371/journal.pgen.1008904
Subject(s) - synapsis , biology , homologous chromosome , meiosis , genetics , atp hydrolysis , mutant , chromosomal crossover , homologous recombination , prophase , microbiology and biotechnology , enzyme , atpase , biochemistry , dna , gene
The conserved ATPase, PCH-2/TRIP13, is required during both the spindle checkpoint and meiotic prophase. However, its specific role in regulating meiotic homolog pairing, synapsis and recombination has been enigmatic. Here, we report that this enzyme is required to proofread meiotic homolog interactions. We generated a mutant version of PCH-2 in C . elegans that binds ATP but cannot hydrolyze it: pch-2 E253Q . In vitro , this mutant can bind a known substrate but is unable to remodel it. This mutation results in some non-homologous synapsis and impaired crossover assurance. Surprisingly, worms with a null mutation in PCH-2’s adapter protein, CMT-1, the ortholog of p31 comet , localize PCH-2 to meiotic chromosomes, exhibit non-homologous synapsis and lose crossover assurance. The similarity in phenotypes between cmt-1 and pch-2 E253Q mutants suggest that PCH-2 can bind its meiotic substrates in the absence of CMT-1, in contrast to its role during the spindle checkpoint, but requires its adapter to hydrolyze ATP and remodel them.