title: Control of meiotic pairing and recombination by chromosomally tethered 26S proteasome.
abstract: During meiosis, paired homologous chromosomes (homologs) become linked via the synaptonemal complex (SC) and crossovers. Crossovers mediate homolog segregation and arise from self-inflicted double-strand breaks (DSBs). Here, we identified a role for the proteasome, the multisubunit protease that degrades proteins in the nucleus and cytoplasm, in homolog juxtaposition and crossing over. Without proteasome function, homologs failed to pair and instead remained associated with nonhomologous chromosomes. Although dispensable for noncrossover formation, a functional proteasome was required for a coordinated transition that entails SC assembly between longitudinally organized chromosome axes and stable strand exchange of crossover-designated DSBs. Notably, proteolytic core and regulatory proteasome particles were recruited to chromosomes by Zip3, the ortholog of mammalian E3 ligase RNF212, and SC protein Zip1 . We conclude that proteasome functions along meiotic chromosomes are evolutionarily conserved.
authors.affiliation: Center for Gene Regulation in Health and Disease and Department of Biological, Geological and Environmental Sciences, Cleveland State University (CSU), Cleveland, OH, USA.
authors.forename: Jasvinder S
authors.initials: JS
authors.lastname: Ahuja
authors.affiliation: Center for Gene Regulation in Health and Disease and Department of Biological, Geological and Environmental Sciences, Cleveland State University (CSU), Cleveland, OH, USA.
authors.forename: Rima
authors.initials: R
authors.lastname: Sandhu
authors.affiliation: Magee-Womens Research Institute, Department of Obstetrics, Gynecology, and Reproductive Sciences, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.
authors.forename: Rana
authors.initials: R
authors.lastname: Mainpal
authors.affiliation: School of Molecular Biosciences, Center for Reproductive Biology, Washington State University, Pullman, WA, USA.
authors.forename: Crystal
authors.initials: C
authors.lastname: Lawson
authors.affiliation: Center for Gene Regulation in Health and Disease and Department of Biological, Geological and Environmental Sciences, Cleveland State University (CSU), Cleveland, OH, USA.
authors.forename: Hanna
authors.initials: H
authors.lastname: Henley
authors.affiliation: School of Molecular Biosciences, Center for Reproductive Biology, Washington State University, Pullman, WA, USA.
authors.forename: Patricia A
authors.initials: PA
authors.lastname: Hunt
authors.affiliation: Magee-Womens Research Institute, Department of Obstetrics, Gynecology, and Reproductive Sciences, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.
authors.forename: Judith L
authors.initials: JL
authors.lastname: Yanowitz
authors.affiliation: Center for Gene Regulation in Health and Disease and Department of Biological, Geological and Environmental Sciences, Cleveland State University (CSU), Cleveland, OH, USA. g.boerner@csuohio.edu.|Case Comprehensive Cancer Center, Case Western Reserve University, Cleveland, OH, USA.|Department of Cancer Biology, Lerner Research Institute, Cleveland Clinic, Cleveland, OH, USA.
authors.forename: G Valentin
authors.initials: GV
authors.lastname: Börner
mesh_terms: D002467:Cell Nucleus / Q000201:enzymology; D023902:Chromosome Pairing; D015825:Chromosomes, Fungal / Q000378:metabolism; D003434:Crossing Over, Genetic; D015853:Cysteine Proteinase Inhibitors / Q000494:pharmacology; D003593:Cytoplasm / Q000201:enzymology; D053903:DNA Breaks, Double-Stranded; D019143:Evolution, Molecular; D007976:Leupeptins / Q000494:pharmacology; D008540:Meiosis / Q000235:genetics / Q000502:physiology*; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex / Q000235:genetics / Q000378:metabolism*; D059748:Proteolysis; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000201:enzymology / Q000502:physiology; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism*; D013573:Synaptonemal Complex / Q000201:enzymology* / Q000235:genetics; D044767:Ubiquitin-Protein Ligases / Q000235:genetics / Q000378:metabolism*
chemical_list: D015853:Cysteine Proteinase Inhibitors; D007976:Leupeptins; D009687:Nuclear Proteins; D029701:Saccharomyces cerevisiae Proteins; C090118:Zip1 protein, S cerevisiae; D044767:Ubiquitin-Protein Ligases; D046988:Proteasome Endopeptidase Complex; C061553:ATP dependent 26S protease; C523917:Zip3 protein, S cerevisiae; C072553:benzyloxycarbonylleucyl-leucyl-leucine aldehyde