Control of meiotic pairing and recombination by chromosomally tethered 26S proteasome.
Science
; 355(6323): 408-411, 2017 01 27.
Article
em En
| MEDLINE
| ID: mdl-28059715
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.
Texto completo:
1
Bases de dados:
MEDLINE
Assunto principal:
Complexo Sinaptonêmico
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Proteínas Nucleares
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Troca Genética
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Proteínas de Saccharomyces cerevisiae
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Ubiquitina-Proteína Ligases
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Complexo de Endopeptidases do Proteassoma
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Meiose
Idioma:
En
Revista:
Science
Ano de publicação:
2017
Tipo de documento:
Article
País de afiliação:
Estados Unidos