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A novel role of Dma1 in regulating forespore membrane assembly and sporulation in fission yeast.

Authors
  • Li, Wen-zhu
  • Yu, Zhi-yong
  • Ma, Peng-fei
  • Wang, Yamei
  • Jin, Quan-wen
Type
Published Article
Journal
Molecular Biology of the Cell
Publisher
American Society for Cell Biology
Publication Date
Dec 01, 2010
Volume
21
Issue
24
Pages
4349–4360
Identifiers
DOI: 10.1091/mbc.E10-01-0079
PMID: 20980623
Source
Medline
License
Unknown

Abstract

In fission yeast Schizosaccharomyces pombe, a diploid mother cell differentiates into an ascus containing four haploid ascospores following meiotic nuclear divisions, through a process called sporulation. Several meiosis-specific proteins of fission yeast have been identified to play essential roles in meiotic progression and sporulation. We report here an unexpected function of mitotic spindle checkpoint protein Dma1 in proper spore formation. Consistent with its function in sporulation, expression of dma1(+) is up-regulated during meiosis I and II. We showed that Dma1 localizes to the SPB during meiosis and the maintenance of this localization at meiosis II depends on septation initiation network (SIN) scaffold proteins Sid4 and Cdc11. Cells lacking Dma1 display defects associated with sporulation but not nuclear division, leading frequently to formation of asci with fewer spores. Our genetic analyses support the notion that Dma1 functions in parallel with the meiosis-specific Sid2-related protein kinase Slk1/Mug27 and the SIN signaling during sporulation, possibly through regulating proper forespore membrane assembly. Our studies therefore revealed a novel function of Dma1 in regulating sporulation in fission yeast.

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