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S. pombe sporulation-specific coiled-coil protein Spo15p is localized to the spindle pole body and essential for its

S Ikemoto1, T Nakamura, M Kubo

  • 1Department of Biology, Graduate School of Science, Osaka City University, Sumiyoshi-ku, Osaka 558-8585, Japan.

Journal of Cell Science
|January 20, 2000
PubMed

Insights

Spo15p is crucial for initiating spore membrane formation in fission yeast, associating with spindle pole bodies throughout the cell cycle. This protein is essential for proper spore development during meiosis.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Spindle pole bodies (SPBs) in Schizosaccharomyces pombe are vital for spindle formation and forespore membrane assembly during meiosis.
  • The spo15 mutant exhibits defects in forespore membrane development, which is essential for spore envelope formation.

Purpose of the Study:

  • To investigate the function of the spo15(+) gene and its encoded protein, Spo15p, in fission yeast.
  • To determine the role of Spo15p in SPB function and spore formation.

Main Methods:

  • Gene disruption and analysis of the spo15 null mutant (spo15delta).
  • Northern and western blot analyses to assess spo15(+) expression.
  • Construction and expression of a spo15-GFP fusion protein.
  • Microscopic observation of mitotic and meiotic spindles, nuclear segregation, and SPB morphology.

Main Results:

  • The spo15 gene disruptant was viable but defective in spore formation.
  • Spo15p is expressed in both meiotic and vegetative cells.
  • Spo15-GFP localized to SPBs, colocalizing with Sad1p.
  • Meiotic divisions, spindle morphology, and nuclear segregation were normal in spo15delta cells.
  • The characteristic transformation of SPB morphology prior to forespore membrane formation was absent in spo15delta cells.

Conclusions:

  • Spo15p is associated with spindle pole bodies throughout the fission yeast life cycle.
  • Spo15p plays an essential role in initiating the formation of spore membranes during meiosis.

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