The synaptonemal complex central region modulates crossover pathways and feedback control of meiotic double-strand break formationopen access
- Authors
- Lee, Min-Su; Higashide, Mika T.; Choi, Hyungseok; Li, Ke; Hong, Soogil; Lee, Kangseok; Shinohara, Akira; Shinohara, Miki; Kim, Keun P.
- Issue Date
- Jul-2021
- Publisher
- NLM (Medline)
- Citation
- Nucleic acids research, v.49, no.13, pp 7537 - 7553
- Pages
- 17
- Journal Title
- Nucleic acids research
- Volume
- 49
- Number
- 13
- Start Page
- 7537
- End Page
- 7553
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/49423
- DOI
- 10.1093/nar/gkab566
- ISSN
- 0305-1048
1362-4962
- Abstract
- The synaptonemal complex (SC) is a proteinaceous structure that mediates homolog engagement and genetic recombination during meiosis. In budding yeast, Zip-Mer-Msh (ZMM) proteins promote crossover (CO) formation and initiate SC formation. During SC elongation, the SUMOylated SC component Ecm11 and the Ecm11-interacting protein Gmc2 facilitate the polymerization of Zip1, an SC central region component. Through physical recombination, cytological, and genetic analyses, we found that ecm11 and gmc2 mutants exhibit chromosome-specific defects in meiotic recombination. CO frequencies on a short chromosome (chromosome III) were reduced, whereas CO and non-crossover frequencies on a long chromosome (chromosome VII) were elevated. Further, in ecm11 and gmc2 mutants, more double-strand breaks (DSBs) were formed on a long chromosome during late prophase I, implying that the Ecm11-Gmc2 (EG) complex is involved in the homeostatic regulation of DSB formation. The EG complex may participate in joint molecule (JM) processing and/or double-Holliday junction resolution for ZMM-dependent CO-designated recombination. Absence of the EG complex ameliorated the JM-processing defect in zmm mutants, suggesting a role for the EG complex in suppressing ZMM-independent recombination. Our results suggest that the SC central region functions as a compartment for sequestering recombination-associated proteins to regulate meiosis specificity during recombination. © The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.
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