SUMO modifications control assembly of synaptonemal complex and polycomplex in meiosis of Saccharomyces cerevisiae.
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.
Cheng
Chung-Hsu
CH
Institute of Biochemical Science, National Taiwan University, Taipei.
Lo
Yu-Hui
YH
Liang
Shu-Shan
SS
Ti
Shih-Chieh
SC
Lin
Feng-Ming
FM
Yeh
Chia-Hui
CH
Huang
Han-Yi
HY
Wang
Ting-Fang
TF
D000595:Amino Acid Sequence; D002503:Centromere / Q000502:physiology; D015825:Chromosomes, Fungal; D008540:Meiosis; D008969:Molecular Sequence Data; D009687:Nuclear Proteins; D011418:Prophase; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D025841:Small Ubiquitin-Related Modifier Proteins / Q000502:physiology*; D013573:Synaptonemal Complex / Q000502:physiology*
D009687:Nuclear Proteins; D029701:Saccharomyces cerevisiae Proteins; D025841:Small Ubiquitin-Related Modifier Proteins; C090118:Zip1 protein, S cerevisiae