SUMO modifications control assembly of synaptonemal complex and polycomplex in meiosis of Saccharomyces cerevisiae
- Chung-Hsu Cheng1,3,4,
- Yu-Hui Lo2,3,4,
- Shu-Shan Liang1,3,
- Shih-Chieh Ti2,
- Feng-Ming Lin3,
- Chia-Hui Yeh3,
- Han-Yi Huang3, and
- Ting-Fang Wang1,2,3,5
- 1 Institute of Biochemical Science, National Taiwan University, Taipei 106, Taiwan;
- 2 Graduate Institute of Life Sciences, National Defense Medical Center, Taipei 114, Taiwan;
- 3 Institute of Biological Chemistry, Academia Sinica,Taipei 115, Taiwan
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↵4 These authors contributed equally to this work.
Abstract
The synaptonemal complex (SC) is a proteinaceous complex that apparently mediates synapsis between homologous chromosomes during meiotic prophase. In Saccharomyces cerevisiae, the Zip1 protein is the integral component of the SC. In the absence of a DNA double-strand break or the SC initiation protein Zip3, Zip1 proteins aggregate to form a polycomplex (PC). In addition, Zip1 is also responsible for DSB-independent nonhomologous centromere coupling at early meiotic prophase. We report here that Zip3 is a SUMO (small ubiquitin-related modifier) E3 ligase and that Zip1 is a binding protein for SUMO-conjugated products. Our results also suggest that at early meiotic prophase, Zip1 interacts with Zip3-independent Smt3 conjugates (e.g., Top2) to promote nonhomologous centromere coupling. At and after mid-prophase, the Zip1 protein begins to associate with Zip3-dependent Smt3 conjugates (e.g., Red1) along meiotic chromosomes in the wild-type cell to form SCs and with Smt3 polymeric chains in the zip3 mutant to form PCs.
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Footnotes
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↵5 Corresponding author.
↵5 E-MAIL tfwang{at}gate.sinica.edu.tw; FAX 886-2-27889759.
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Supplemental material is available at http://www.genesdev.org.
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Article published online ahead of print. Article and publication date are online at http://www.genesdev.org/cgi/doi/10.1101/gad.1430406
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- Received March 17, 2006.
- Accepted June 2, 2006.
- Copyright © 2006, Cold Spring Harbor Laboratory Press