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2 "soo1-1"
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Research Support, Non-U.S. Gov't
Enhanced Secretion of Cell Wall Bound Enolase into Culture Medium by the soo1-1 Mutation of Saccharomyces cerevisiae
Ki-Hyun Kim , Hee-Moon Park
J. Microbiol. 2004;42(3):248-252.
DOI: https://doi.org/2080 [pii]
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AbstractAbstract
In order to identify the protein(s) secreted into culture medium by the soo1-1/ret1-1 mutation of Saccharomyces cerevisiae, proteins from the culture medium of cells grown at permissive (28^oC) and non-permissive temperatures (37^oC), were analyzed. Comparison of protein bands separated by SDS-PAGE identified a prominent band of 47-kDa band from a mutant grown at 37^oC. N-terminal amino acid sequencing of this 47-kDa protein showed high identity with enolases 1 and 2. Western blot analysis revealed that most of the cell wall-bound enolase was released into the culture medium of the mutant grown at 37^oC, some of which were separated as those with lower molecular weights. Our results, presented here, indicate the impairment of cell wall enolase biogenesis and assembly by the soo1-1/ret1-1 mutation of S. cerevisiae.
Characterization of Cell Wall Proteins from the soo1-1/ret1-1 Mutant of Saccharomyces cerevisiae
Dong-Won Lee , Ki-Hyun Kim , Se-Chul Chun , Hee-Moon Park
J. Microbiol. 2002;40(3):219-223.
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AbstractAbstract
In order to investigate the function of Soo1p/[alpha]-COP during post-translational modification and intracellular transport of cell wall proteins in Saccharomyces cerevisiae, cell wall proteins from the soo1-1/ret1-1 mutant cells were analyzed. SDS-PAGE analysis of biotin labeled cell wall proteins suggested that the soo1-1 mutation impairs post-translational modification of cell wall proteins, such as N- and/or O-glycosylation. Analysis of cell wall proteins with antibodies against [beta]-1,3-glucan and [beta]-1,6-glucan revealed alteration of the linkage between cell wall proteins and [beta]-glucans in the soo1-1 mutant cells. Compositional sugar analysis of the cell wall proteins also suggested that the soo1-1 mutation impairs glycosylation of cell wall protein in the ER, which is crucial for the maintenance of cell wall integrity.

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