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A meiotic XPF-ERCC1-like complex recognizes joint molecule recombination intermediates to promote crossover formation.

  • De Muyt A UMR3244, Centre Nationnal de la Recherche Scientifique (CNRS), Institut Curie, PSL (Paris Sciences and Letters) Research University, 75005 Paris, France.
  • Pyatnitskaya A UMR3244, Centre Nationnal de la Recherche Scientifique (CNRS), Institut Curie, PSL (Paris Sciences and Letters) Research University, 75005 Paris, France.
  • Andréani J Institut de Biologie Intégrative de la Cellule (I2BC), Institut de biologie et de technologies de Saclay (iBiTec-S), Commissariat à l'Énergie Atomique et aux Énergies Alternatives (CEA), UMR9198, CNRS, Université Paris-Sud, 91190 Gif-sur-Yvette, France.
  • Ranjha L Institute for Research in Biomedicine, Università della Svizzera italiana, 6500 Bellinzona, Switzerland.
  • Ramus C University of Grenoble Alpes, CEA, Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de Biosciences et Biotechnologies de Grenoble (BIG-BGE), 38000 Grenoble, France.
  • Laureau R UMR3244, Centre Nationnal de la Recherche Scientifique (CNRS), Institut Curie, PSL (Paris Sciences and Letters) Research University, 75005 Paris, France.
  • Fernandez-Vega A UMR3244, Centre Nationnal de la Recherche Scientifique (CNRS), Institut Curie, PSL (Paris Sciences and Letters) Research University, 75005 Paris, France.
  • Holoch D Université Pierre et Marie Curie (UPMC), 75005 Paris, France.
  • Girard E Institut Curie, PSL Research University, Mines ParisTech, U900, INSERM, 75005 Paris, France.
  • Govin J University of Grenoble Alpes, CEA, Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de Biosciences et Biotechnologies de Grenoble (BIG-BGE), 38000 Grenoble, France.
  • Margueron R Université Pierre et Marie Curie (UPMC), 75005 Paris, France.
  • Couté Y University of Grenoble Alpes, CEA, Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de Biosciences et Biotechnologies de Grenoble (BIG-BGE), 38000 Grenoble, France.
  • Cejka P Institute for Research in Biomedicine, Università della Svizzera italiana, 6500 Bellinzona, Switzerland.
  • Guérois R Institut de Biologie Intégrative de la Cellule (I2BC), Institut de biologie et de technologies de Saclay (iBiTec-S), Commissariat à l'Énergie Atomique et aux Énergies Alternatives (CEA), UMR9198, CNRS, Université Paris-Sud, 91190 Gif-sur-Yvette, France.
  • Borde V UMR3244, Centre Nationnal de la Recherche Scientifique (CNRS), Institut Curie, PSL (Paris Sciences and Letters) Research University, 75005 Paris, France.
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  • 2018-02-15
Published in:
  • Genes & development. - 2018
XPF–ERCC1
Zip2–Zip4–Spo16 complex
crossover
homologous recombination
meiosis
synaptonemal complex
Chromosomal Proteins, Non-Histone
Chromosomes, Fungal
Crossing Over, Genetic
DNA
DNA Breaks, Double-Stranded
DNA-Binding Proteins
Endodeoxyribonucleases
Meiosis
Microtubule-Associated Proteins
Protein Domains
Saccharomyces cerevisiae Proteins
English Meiotic crossover formation requires the stabilization of early recombination intermediates by a set of proteins and occurs within the environment of the chromosome axis, a structure important for the regulation of meiotic recombination events. The molecular mechanisms underlying and connecting crossover recombination and axis localization are elusive. Here, we identified the ZZS (Zip2-Zip4-Spo16) complex, required for crossover formation, which carries two distinct activities: one provided by Zip4, which acts as hub through physical interactions with components of the chromosome axis and the crossover machinery, and the other carried by Zip2 and Spo16, which preferentially bind branched DNA molecules in vitro. We found that Zip2 and Spo16 share structural similarities to the structure-specific XPF-ERCC1 nuclease, although it lacks endonuclease activity. The XPF domain of Zip2 is required for crossover formation, suggesting that, together with Spo16, it has a noncatalytic DNA recognition function. Our results suggest that the ZZS complex shepherds recombination intermediates toward crossovers as a dynamic structural module that connects recombination events to the chromosome axis. The identification of the ZZS complex improves our understanding of the various activities required for crossover implementation and is likely applicable to other organisms, including mammals.
Language
  • English
Open access status
gold
Identifiers
Persistent URL
https://sonar.ch/global/documents/279069
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