ArticleProceedings of the National Academy of Sciences of the United States of America2009
Oxidoreductase activity of oligosaccharyltransferase subunits Ost3p and Ost6p defines site-specific glycosylation efficiency.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.
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Who cites it
69 citing papers in PubMed, 124 citations in OpenAlex.
- N-glycan-dependent protein maturation and quality control in the ER.Nature reviews. Molecular cell biology · 2025Review
- Robust and Reproducible Monoclonal Antibody Production Using a Transgenic Silkworm System.International journal of molecular sciences · 2025Article
- Structural Insights into the Protein Mannosyltransferase from Mycobacterium tuberculosis reveal a WW-Domain-Like Protein Motif in Bacteria.Communications biology · 2025Article
- Expanding Asgard members in the domain of Archaea sheds new light on the origin of eukaryotes.Science China. Life sciences · 2022Article
- Hidden Relationships betweenInternational journal of molecular sciences · 2022Review
- TorsinA folding and N-linked glycosylation are sensitive to redox homeostasis.Biochimica et biophysica acta. Molecular cell research · 2021Article
- Protein N-glycosylation and O-mannosylation are catalyzed by two evolutionarily related GT-C glycosyltransferases.Current opinion in structural biology · 2021Review
- The translocon-associated protein (TRAP) complex regulates quality control of N-linked glycosylation during ER stress.Science advances · 2021Article
- Recent Progress in Structural Studies on the GT-C Superfamily of Protein Glycosyltransferases.Sub-cellular biochemistry · 2021Review
- Uncoupling the hydrolysis of lipid-linked oligosaccharide from the oligosaccharyl transfer reaction by point mutations in yeast oligosaccharyltransferase.The Journal of biological chemistry · 2020Article
- Review
- An Update on XMEN Disease.Journal of clinical immunology · 2020Review
- Structural Insight into the Mechanism ofBiomolecules · 2020Review
- Comparative and evolutionary analyses of the divergence of plant oligosaccharyltransferase STT3 isoforms.FEBS open bio · 2020Article
- Defective glycosylation and multisystem abnormalities characterize the primary immunodeficiency XMEN disease.The Journal of clinical investigation · 2020Article
- Asparagine-linked glycosylation is not directly coupled to protein translocation across the endoplasmic reticulum inMolecular biology of the cell · 2019Article
- Magnesium transporter 1 (MAGT1) deficiency causes selective defects inThe Journal of biological chemistry · 2019Article
- Quantitative glycoproteomics reveals new classes of STT3A- and STT3B-dependent N-glycosylation sites.The Journal of cell biology · 2019Article
- Mutations inProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Oligosaccharyltransferase structures provide novel insight into the mechanism of asparagine-linked glycosylation in prokaryotic and eukaryotic cells.Glycobiology · 2019Review
9 more citing papers are in PubMed but not listed here.
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.