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Vol. 14, Issue 3, 1109-1124, March 2003
and
*Department of Biology, Graduate School of Science, Osaka
City University, Sugimoto, Sumiyoshi-ku, Osaka 558-8585, Japan; and
The Schizosaccharomyces pombe spo14-B221 mutant was
originally isolated as a sporulation-deficient mutant. However, the
spo14+ gene is essential for cell
viability and growth. spo14+ is
identical to the previously characterized
stl1+ gene encoding a putative
homologue of Saccharomyces cerevisiae Sec12, which is
essential for protein transport from the endoplasmic reticulum (ER) to
the Golgi apparatus. In the spo14 mutant cells, ER-like
membranes were accumulated beneath the plasma membrane and the ER/Golgi
shuttling protein Rer1 remained in the ER. Sec12 is a guanine
nucleotide exchange factor for the Sar1 GTPase. Overproduction of
psr1+ coding for an S.
pombe Sar1 homologue suppressed both the sporulation defect of
spo14-B221 and cold-sensitive growth of newly isolated spo14-6 and spo14-7 mutants. These
results indicate that Spo14 is involved in early steps of the protein
secretory pathway. The spo14-B221 allele carries a
single nucleotide change in the branch point consensus of the fifth
intron, which reduces the abundance of the spo14 mRNA.
During meiosis II, the forespore membrane was initiated near spindle
pole bodies; however, subsequent extension of the membrane was arrested
before its closure into a sac. We conclude that Spo14 is responsible
for the assembly of the forespore membrane by supplying membrane vesicles.
Department of Integrated Biosciences, Graduate
School of Frontier Science, University of Tokyo, Kashiwa, Chiba
277-8562, Japan.
Corresponding author. E-mail address:
shimoda{at}sci.osaka-cu.ac.jp.
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