PCH-2 collaborates with CMT-1 to proofread meiotic homolog interactions
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 interact...
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| creator | Giacopazzi, Stefani Vong, Daniel Devigne, Alice Bhalla, Needhi Barsh, Gregory S Libuda, Diana E |
| description | 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.sup.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.sup.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.sup.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. |
| doi_str_mv | 10.1371/journal.pgen.1008904 |
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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.sup.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.sup.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.sup.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.</description><identifier>ISSN: 1553-7404</identifier><identifier>ISSN: 1553-7390</identifier><identifier>EISSN: 1553-7404</identifier><identifier>DOI: 10.1371/journal.pgen.1008904</identifier><identifier>PMID: 32730253</identifier><language>eng</language><publisher>San Francisco: Public Library of Science</publisher><subject>Adapter proteins ; Adenosine triphosphatase ; Analysis ; Apoptosis ; ATPases ; Biology and Life Sciences ; Caenorhabditis elegans ; Cell division ; Defects ; Developmental biology ; Gene mutation ; Genetic aspects ; Insects ; Localization ; Meiosis ; Mutants ; Mutation ; Phenotypes ; Prophase ; Recombination ; Research and Analysis Methods ; X chromosomes ; Yeast</subject><ispartof>PLoS genetics, 2020-07, Vol.16 (7), p.e1008904-e1008904</ispartof><rights>COPYRIGHT 2020 Public Library of Science</rights><rights>2020 Giacopazzi et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. 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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.sup.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.sup.comet, localize PCH-2 to meiotic chromosomes, exhibit non-homologous synapsis and lose crossover assurance. 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| subjects | Adapter proteins Adenosine triphosphatase Analysis Apoptosis ATPases Biology and Life Sciences Caenorhabditis elegans Cell division Defects Developmental biology Gene mutation Genetic aspects Insects Localization Meiosis Mutants Mutation Phenotypes Prophase Recombination Research and Analysis Methods X chromosomes Yeast |
| title | PCH-2 collaborates with CMT-1 to proofread meiotic homolog interactions |
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