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Mol. Cells 2011; 31(2): 151-158
Published online November 25, 2010
https://doi.org/10.1007/s10059-011-0012-z
© The Korean Society for Molecular and Cellular Biology
Effect of Saccharomyces cerevisiae ret1-1 Mutation on Glycosylation and Localization of the Secretome
Correspondence to : *Correspondence: hmpark@cnu.ac.kr
To study the effect of the ret1-1 mutation on the secre-tome, the glycosylation patterns and locations of the secretory proteins and glycosyltransferases responsible for glycosylation were investigated. Analyses of secretory proteins and cell wall-associated glycoproteins showed severe impairment of glycosylation in this mutant. Results from 2D- polyacrylamide gel electrophoresis (PAGE) indicated defects in the glycosylation and cellular localization of SDS-soluble cell wall proteins. Localization of RFP-tagged glycosyltransferase proteins in ret1-1 indicated an impairment of Golgi-to retrograde transport at a non-permissive temperature. Thus, impaired glycosylation caused by the mislocalization of ER resident proteins appears to be responsible for the alterations in the secretome and the increased sensitivity to ER stress in ret1-1 mutant cells.
Keywords glycosylation, localization, ret1-1 mutation, Saccharomyces cerevisiae, secretome
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Research Article
Mol. Cells 2011; 31(2): 151-158
Published online February 28, 2011 https://doi.org/10.1007/s10059-011-0012-z
Copyright © The Korean Society for Molecular and Cellular Biology.
Effect of Saccharomyces cerevisiae ret1-1 Mutation on Glycosylation and Localization of the Secretome
Ki-Hyun Kim, Eun-Kyung Kim, Su-Jin Kim, Yun-Hee Park, and Hee-Moon Park*
Department of Microbiology and Molecular Biology, College of Bioscience and Biotechnology, Chungnam National University, Daejeon 305-764, Korea
Correspondence to:*Correspondence: hmpark@cnu.ac.kr
Abstract
To study the effect of the ret1-1 mutation on the secre-tome, the glycosylation patterns and locations of the secretory proteins and glycosyltransferases responsible for glycosylation were investigated. Analyses of secretory proteins and cell wall-associated glycoproteins showed severe impairment of glycosylation in this mutant. Results from 2D- polyacrylamide gel electrophoresis (PAGE) indicated defects in the glycosylation and cellular localization of SDS-soluble cell wall proteins. Localization of RFP-tagged glycosyltransferase proteins in ret1-1 indicated an impairment of Golgi-to retrograde transport at a non-permissive temperature. Thus, impaired glycosylation caused by the mislocalization of ER resident proteins appears to be responsible for the alterations in the secretome and the increased sensitivity to ER stress in ret1-1 mutant cells.
Keywords: glycosylation, localization, ret1-1 mutation, Saccharomyces cerevisiae, secretome
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