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Vol. 12, Issue 4, 901-917, April 2001
and
*Department of Biology, Graduate School of Science, Osaka City
University, Sumiyoshi-ku, Osaka 558-8585, Japan;
The Schizosaccharomyces pombe spo20-KC104 mutation
was originally isolated in a screen for sporulation-deficient mutants, and the spo20-KC104 mutant exhibits
temperature-sensitive growth. Herein, we report that S.
pombe, spo20+ is essential for
fission yeast cell viability and is constitutively expressed throughout
the life cycle. We also demonstrate that the
spo20+ gene product is structurally
homologous to Saccharomyces cerevisiae Sec14, the major
phosphatidylinositol transfer protein of budding yeast. This
structural homology translates to a significant degree of functional
relatedness because reciprocal complementation experiments demonstrate
that each protein is able to fulfill the essential function of the
other. Moreover, biochemical experiments show that, like Sec14, Spo20
is a phosphatidylinositol/phosphatidylcholine-transfer protein.
That Spo20 is required for Golgi secretory function in vegetative cells
is indicated by our demonstration that the spo20-KC104 mutant accumulates aberrant Golgi cisternae at restrictive
temperatures. However, a second phenotype observed in Spo20-deficient
fission yeast is arrest of cell division before completion of cell
separation. Consistent with a direct role for Spo20 in controlling cell
septation in vegetatively growing cells, localization experiments
reveal that Spo20 preferentially localizes to the cell poles and to
sites of septation of fission yeast cells. We also report that, when fission yeasts are challenged with nitrogen starvation, Spo20 translocates to the nucleus. This nuclear localization persists during
conjugation and meiosis. On completion of meiosis, Spo20 translocates
to forespore membranes, and it is the assembly of forespore membranes
that is abnormal in spo20-KC104 cells. In such mutants,
a considerable fraction of forming prespores fail to encapsulate the
haploid nucleus. Our results indicate that Spo20 regulates the
formation of specialized membrane structures in addition to its
recognized role in regulating Golgi secretory function.
Institute of Molecular and Cellular Biosciences, The
University of Tokyo, Bunkyo-ku, Tokyo 113-0032; and
Department of Cell Biology, University of Alabama at
Birmingham, Birmingham, Alabama 35294-0005
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