한빛사논문
Min-Su Lee1,†, Mika T. Higashide2,†, Hyungseok Choi1,†, Ke Li2,3, Soogil Hong1, Kangseok Lee1, Akira Shinohara2, Miki Shinohara2,3,4,* and Keun P. Kim1,*
1Department of Life Science, Chung-Ang University, Seoul 06974, South Korea, 2Institute for Protein Research, Osaka University, Osaka 565-0871, Japan, 3Graduate School of Agriculture, Kindai University, Nara 631-8505, Japan and 4Agricultural Technology and Innovation Research Institute, Kindai University, Nara 631-8505, Japan
*To whom correspondence should be addressed.
†The authors wish it to be known that, in their opinion, the first three authors should be regarded as Joint First Authors.
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.
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