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Vol. 12, Issue 12, 3955-3972, December 2001
and
*Department of Biology, Graduate School of Science, Osaka City
University, Osaka 558-8585, Japan; and Formation of the forespore membrane, which becomes the plasma
membrane of spores, is an intriguing step in the sporulation of the
fission yeast Schizosaccharomyces pombe. Here we report two novel proteins that localize to the forespore membrane.
spo3+ encodes a potential membrane protein,
which was expressed only during sporulation. Green fluorescent protein
(GFP) fusion revealed that Spo3 localized to the forespore membrane.
The spo3 disruptant was viable and executed meiotic
nuclear divisions as efficiently as the wild type but did not form
spores. One of the spo3 alleles, spo3-KC51, was dose-dependently suppressed by
psy1+, which encodes a protein similar
to mammalian syntaxin-1A, a component of the plasma membrane
docking/fusion complex. psy1+ was essential
for vegetative growth, and its transcription was enhanced during
sporulation. As expected, Psy1 localized to the plasma membrane during
vegetative growth. Interestingly, Psy1 on the plasma membrane
disappeared immediately after first meiotic division and relocalized to
the forespore membrane as the second division initiated. In the
spo3 null mutant, the forespore membrane was initiated
but failed to develop a normal morphology. Electron microscopy revealed
that membrane vesicles were accumulated in the cytoplasm of immature
spo3Department of
Integrated Biosciences, Graduate School of Frontier Science, University
of Tokyo, Chiba 277-8562, Japan
asci. These results suggest that Spo3 is a key
component of the forespore membrane and is essential for its assembly
acting in collaboration with the syntaxin-like protein.
The first two authors contributed equally to this work.
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