Journal
SCIENCE
Volume 355, Issue 6323, Pages 408-411Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aaf4778
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Funding
- NIH [R15GM099056, R01GM104007, R01HD083177]
- CSU
- John Vitullo's Bridge Funding Program
- Center for Gene Regulation in Health and Disease
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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.
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