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Vol. 180, Issue 13, 3381-3387, July 1, 1998
National Research Institute of Brewing,
Kagamiyama, Higashihiroshima 739-0046, Japan
A 260-kDa structural cell wall protein was purified from sodium
dodecyl sulfate-treated cell walls of Saccharomyces
cerevisiae by incubation with Rarobacter faecitabidus
protease I, which is a yeast-lytic enzyme. Amino acid sequence analysis
revealed that this protein is the product of the SED1 gene.
SED1 was formerly identified as a multicopy suppressor of
erd2, which encodes a protein involved in retrieval of
luminal endoplasmic reticulum proteins from the secretory pathway.
Sed1p is very rich in threonine and serine and, like other structural
cell wall proteins, contains a putative signal sequence for the
addition of a glycosylphosphatidylinositol anchor. However, the fact
that Sed1p, unlike other cell wall proteins, has six cysteines and
seven putative N-glycosylation sites suggests that Sed1p belongs to a
new family of cell wall proteins. Epitope-tagged Sed1p was detected in
a
Sed1p Is a Major Cell Wall Protein of
Saccharomyces cerevisiae in the Stationary Phase and Is
Involved in Lytic Enzyme Resistance
-1,3-glucanase extract of cell walls by immunoblot analysis,
suggesting that Sed1p is a glucanase-extractable cell wall protein. The
expression of Sed1p mRNA increased in the stationary phase and was
accompanied by an increase in the Sed1p content of cell walls.
Disruption of SED1 had no effect on exponentially growing
cells but made stationary-phase cells sensitive to Zymolyase. These
results indicate that Sed1p is a major structural cell wall protein in
stationary-phase cells and is required for lytic enzyme resistance.
Copyright © 1998 by American Society for Microbiology
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