Characterization of Yeast sar1 Temperature-Sensitive Mutants, Which Are Defective in Protein Transport from the Endoplasmic Reticulum

1996 ◽  
Vol 120 (2) ◽  
pp. 452-458 ◽  
Author(s):  
T. Yamanush ◽  
A. Hirata ◽  
T. Oka ◽  
A. Nakano
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Transport ◽  
Temperature Sensitive ◽  
Temperature Sensitive Mutants

Biochemical characterization of poliovirus type 1 temperature-sensitive mutants

Virology ◽  
1984 ◽  
Vol 139 (2) ◽  
pp. 403-407 ◽  
Author(s):  
Christine Bellocq ◽  
Henri Agut ◽  
Sylvie Van Der Werf ◽  
Marc Girard
Keyword(s):  
Biochemical Characterization ◽  
Temperature Sensitive ◽  
Poliovirus Type ◽  
Temperature Sensitive Mutants

Isolation and partial characterization of temperature-sensitive mutants of Mengo virus

Virology ◽  
1976 ◽  
Vol 70 (1) ◽  
pp. 190-194 ◽  
Author(s):  
Donald N. Downer ◽  
Sylvia Sunderland ◽  
John S. Colter
Keyword(s):  
Partial Characterization ◽  
Temperature Sensitive ◽  
Temperature Sensitive Mutants ◽  
Mengo Virus

Genetic and biochemical studies of asparagine-linked oligosaccharide assembly

1982 ◽  
Vol 300 (1099) ◽  
pp. 207-223 ◽  
Keyword(s):  
Protein Synthesis ◽  
Temperature Sensitive ◽  
Temperature Sensitive Mutants ◽  
Isolation And Characterization ◽  
Oligosaccharide Processing ◽  
Biochemical Studies ◽  
The Common ◽  
Specific Lipid ◽  
Temperature Sensitive Phenotype

The formation of N -glycosidic linkages of eukaryotic glycoproteins involves the assembly of a specific lipid-linked precursor oligosaccharide in the endoplasmic reticulum. This oligosaccharide is transferred from the lipid carrier to appropriate asparagine residues during protein synthesis. The protein-linked oligosaccharide then undergoes processing reactions that include both removal and addition of carbohydrate residues. In this paper we report recent studies from our laboratory on the synthesis of asparagine-linked oligosaccharides. In the first part we describe the isolation and characterization of temperature-sensitive mutants of yeast blocked at specific stages in the assembly of the lipid-linked oligosaccharide. In addition, we are using these mutants to clone the genes for the enzymes in this pathway by complementation of the temperature-sensitive phenotype. The second part deals with the topography of asparagine-linked oligosaccharide assembly. Our studies on the transmembrane movement of sugar residues during the assembly of secreted glycoproteins from cytoplasmic precursors are presented. Finally, experiments on the control of protein-linked oligosaccharide processing are described. Recent data are presented on the problem of how specific oligosaccharides are assembled from the common precursors at individual sites on glycoproteins.

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