SUMO modifications control assembly of synaptonemal complex and polycomplex in meiosis of Saccharomyces cerevisiae

  1. Chung-Hsu Cheng1,3,4,
  2. Yu-Hui Lo2,3,4,
  3. Shu-Shan Liang1,3,
  4. Shih-Chieh Ti2,
  5. Feng-Ming Lin3,
  6. Chia-Hui Yeh3,
  7. Han-Yi Huang3, and
  8. Ting-Fang Wang1,2,3,5
  1. 1 Institute of Biochemical Science, National Taiwan University, Taipei 106, Taiwan;
  2. 2 Graduate Institute of Life Sciences, National Defense Medical Center, Taipei 114, Taiwan;
  3. 3 Institute of Biological Chemistry, Academia Sinica,Taipei 115, Taiwan
  1. 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.

Keywords

Footnotes

Related Article

| Table of Contents

Life Science Alliance