Oxidoreductase activity of oligosaccharyltransferase subunits Ost3p and Ost6p defines site-specific glycosylation efficiency

Schulz, Benjamin L., Stirnimann, Christian U., Grimshaw, John P. A., Brozzo, Maurice S., Fritsch, Fabienne, Mohorko, Elisabeth, Capitani, Guido, Glockshuber, Rudi, Grütter, Markus G. and Aebi, Markus (2009) Oxidoreductase activity of oligosaccharyltransferase subunits Ost3p and Ost6p defines site-specific glycosylation efficiency. PNAS, 106 27: 11061-11066. doi:10.1073/pnas.0812515106


Author Schulz, Benjamin L.
Stirnimann, Christian U.
Grimshaw, John P. A.
Brozzo, Maurice S.
Fritsch, Fabienne
Mohorko, Elisabeth
Capitani, Guido
Glockshuber, Rudi
Grütter, Markus G.
Aebi, Markus
Title Oxidoreductase activity of oligosaccharyltransferase subunits Ost3p and Ost6p defines site-specific glycosylation efficiency
Journal name PNAS   Check publisher's open access policy
ISSN 0027-8424
1091-6490
Publication date 2009-07-07
Sub-type Article (original research)
DOI 10.1073/pnas.0812515106
Open Access Status Not Open Access
Volume 106
Issue 27
Start page 11061
End page 11066
Total pages 6
Place of publication Washington, DC, United States
Publisher National Academy of Sciences
Language eng
Subject 06 Biological Sciences
Abstract Asparagine-linked glycosylation is a common posttranslational modification of diverse secretory and membrane proteins in eukaryotes, where it is catalyzed by the multiprotein complex oligosaccharyltransferase. The functions of the protein subunits of oligoasccharyltransferase, apart from the catalytic Stt3p, are ill defined. Here we describe functional and structural investigations of the Ost3/6p components of the yeast enzyme. Genetic, biochemical and structural analyses of the lumenal domain of Ost6p revealed oxidoreductase activity mediated by a thioredoxin-like fold with a distinctive active-site loop that changed conformation with redox state. We found that mutation of the active-site cysteine residues of Ost6p and its paralogue Ost3p affected the glycosylation efficiency of a subset of glycosylation sites. Our results show that eukaryotic oligosaccharyltransferase is a multifunctional enzyme that acts at the crossroads of protein modification and protein folding.
Keyword Crystal structure
Mass spectrometrymass spectrometry
N-glycosylation
Protein folding
Thioredoxin-like protein
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown
Additional Notes Proceedings of the National Academy of Sciences of the United States of America

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 66 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 67 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Fri, 24 Jul 2009, 02:13:21 EST by Mr Benjamin Schulz on behalf of School of Chemistry & Molecular Biosciences