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PMID: 1903839 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The yeast SLY gene products, suppressors of defects in the essential GTP-binding Ypt1 protein, may act in endoplasmic reticulum-to-Golgi transport.

Molecular and cellular biology ·Vol. 11 ·No. 6 ·1991-06-00 ·Pages 2980-93

Ossig R, Dascher C, Trepte HH, Schmitt HD, Gallwitz D

Abstract

It has been shown previously that defects in the essential GTP-binding protein, Ypt1p, lead to a block in protein transport from the endoplasmic reticulum (ER) to the Golgi apparatus in the yeast Saccharomyces cerevisiae. Here we report that four newly discovered suppressors of YPT1 deletion (SLY1-20, SLY2, SLY12, and SLY41) to a varying degree restore ER-to-Golgi transport defects in cells lacking Ypt1p. These suppressors also partially complement the sec21-1 and sec22-3 mutants which lead to a defect early in the secretory pathway. Sly1p-depleted cells, as well as a conditional lethal sly2 null mutant at nonpermissive temperatures, accumulate ER membranes and core-glycosylated invertase and carboxypeptidase Y. The sly2 null mutant under restrictive conditions (37 degrees C) can be rescued by the multicopy suppressor SLY12 and the single-copy suppressor SLY1-20, indicating that these three SLY genes functionally interact. Sly2p is shown to be an integral membrane protein.

Related Genes
SLY
MeSH Terms
Diploidy Endoplasmic Reticulum/metabolism Fungal Proteins/genetics,isolation & purification GTP-Binding Proteins/genetics Genes, Fungal Genes, Suppressor Genotype Glycoside Hydrolases/metabolism Golgi Apparatus/metabolism Haploidy Kinetics Plasmids Proteins/genetics,isolation & purification,metabolism Restriction Mapping Saccharomyces cerevisiae/genetics,physiology,ultrastructure Saccharomyces cerevisiae Proteins beta-Fructofuranosidase rab GTP-Binding Proteins
Chemicals
Fungal Proteins Proteins Saccharomyces cerevisiae Proteins Glycoside Hydrolases beta-Fructofuranosidase GTP-Binding Proteins YPT1 protein, S cerevisiae rab GTP-Binding Proteins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Ossig R
Department of Molecular Genetics, Max-Planck-Institute for Biophysical Chemistry, Göttingen, Federal Republic of Germany.
Dascher C
Trepte H H
Schmitt H D
Gallwitz D
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
Published
1991-06-00
Pages
2980-93
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC360128
Subset
IM
Corrections
CommentIn
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