Effect of Saccharomyces cerevisiae ret1-1 mutation on glycosylation and localization of the secretome.
To study the effect of the ret1-1 mutation on the secretome, 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.
Department of Microbiology and Molecular Biology, College of Bioscience and Biotechnology, Chungnam National University, Daejeon, Korea.
Ki-Hyun
KH
Kim
Eun-Kyung
EK
Kim
Su-Jin
SJ
Kim
Yun-Hee
YH
Park
Hee-Moon
HM
Park
D015415:Biomarkers / Q000378:metabolism; D002473:Cell Wall / Q000378:metabolism; D003470:Culture Media; D015180:Electrophoresis, Gel, Two-Dimensional; D004721:Endoplasmic Reticulum / Q000378:metabolism; D006031:Glycosylation; D015151:Immunoblotting; D009154:Mutation / Q000235:genetics*; D011499:Protein Processing, Post-Translational; D021381:Protein Transport; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics* / Q000378:metabolism*; D055571:Secretory Pathway; D056811:Unfolded Protein Response
D015415:Biomarkers; D003470:Culture Media; D029701:Saccharomyces cerevisiae Proteins