- Effects of Mutations in the WD40 Domain of α-COP on Its Interaction with the COPI Coatomer in Saccharomyces cerevisiae
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Ki-Hyun Kim , Eun Kyung Kim , Ki Young Jeong , Yun-Hee Park , Hee-Moon Park
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J. Microbiol. 2012;50(2):256-262. Published online April 27, 2012
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DOI: https://doi.org/10.1007/s12275-012-1326-z
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 Abstract
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Replacement of glycine 227 in the fifth WD40 motif of
α-COP/Ret1p/Soo1p by charged or aromatic amino acids is
responsible for the temperature-dependent osmo-sensitivity
of Saccharomyces cerevisiae, while truncations of WD40
motifs exerted a reduction in cell growth rate and impairment
in assembly of cell-wall associated proteins such as
enolase and Gas1p. Yeast two-hybrid analysis revealed that
the ret1-1/soo1-1 mutation of α-COP abolished the interaction
with β- and ε-COP, respectively, and that the interaction
between α-COP and β-COP relied on the WD40 domain
of α-COP. Furthermore, although the WD40 domain
is dispensable for interaction of α-COP with ε-COP, structural
alterations in the WD40 domain could impair the
interaction.
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Citations
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Journal of Agricultural and Food Chemistry.2021; 69(12): 3677. CrossRef - Identification and expression profile of an alpha-COPI homologous gene (COPA1) involved in high irradiance and salinity stress in Haematococcus pluvialis
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The Korean Journal of Mycology.2012; 40(4): 224. CrossRef
- Enhanced Secretion of Cell Wall Bound Enolase into Culture Medium by the soo1-1 Mutation of Saccharomyces cerevisiae
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Ki-Hyun Kim , Hee-Moon Park
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J. Microbiol. 2004;42(3):248-252.
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DOI: https://doi.org/2080 [pii]
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Abstract
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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
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Dong-Won Lee , Ki-Hyun Kim , Se-Chul Chun , Hee-Moon Park
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J. Microbiol. 2002;40(3):219-223.
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Abstract
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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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