ArticleBiochemistry2014
The middle X residue influences cotranslational N-glycosylation consensus site skipping.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- N-linked glycosylation sites with low occupancy support sustained circulation of the A(H3N2) influenza A virus in the human population.Journal of virology · 2026Article
- Neuroligins and Neuropathic Pain: Insights into Synaptic Plasticity and Pain Transmission.Biology · 2026Review
- Extensive Hypoglycosylation of Serum N-Glycoproteins in SRD5A3 Deficiency.Journal of inherited metabolic disease · 2026Article
- N-glycosylation in the SERPIN domain of the C1-esterase inhibitor in hereditary angioedema.JCI insight · 2025Article
- LacdiNAc to LacNAc: remodelling of bovine α-lactalbumin N-glycosylation during the transition from colostrum to mature milk.Glycobiology · 2024Article
- Acceptors stability modulates the efficiency of post-translational protein N-glycosylation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024Article
- A complement C4-derived glycopeptide is a biomarker for PMM2-CDG.JCI insight · 2024Article
- The role of N-glycosylation in spike antigenicity for the SARS-CoV-2 gamma variant.Glycobiology · 2024Article
- N-glycosylation as a eukaryotic protective mechanism against protein aggregation.Science advances · 2024Article
- Variations within the Glycan Shield of SARS-CoV-2 Impact Viral Spike Dynamics.Journal of molecular biology · 2023Article
- Site-to-site cross-talk in OST-B glycosylation of hCEACAM1-IgV.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Enhancing the Thermostability of Phytase to Boiling Point by Evolution-Guided Design.Applied and environmental microbiology · 2022Article
- Involvement of testicular N-glycoproteome heterogeneity in seasonal spermatogenesis of the American mink (Frontiers in veterinary science · 2022Article
- Design of an improved universal signal peptide based on the α-factor mating secretion signal for enzyme production in yeast.Cellular and molecular life sciences : CMLS · 2021Article
- The Role of Substrate Mediated Allostery in the Catalytic Competency of the Bacterial Oligosaccharyltransferase PglB.Frontiers in molecular biosciences · 2021Article
- Human variant of scavenger receptor BI (R174C) exhibits impaired cholesterol transport functions.Journal of lipid research · 2021Article
- Structural Insight into the Mechanism ofBiomolecules · 2020Review
- Asparagine-linked glycosylation is not directly coupled to protein translocation across the endoplasmic reticulum inMolecular biology of the cell · 2019Article
- Quantitative glycoproteomics reveals new classes of STT3A- and STT3B-dependent N-glycosylation sites.The Journal of cell biology · 2019Article
- UniqueJournal of biological engineering · 2019Article
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Authors and funding
2 authors.
Funding
Abstract
Asparagine (N)-linked glycosylation is essential for efficient protein folding in the endoplasmic reticulum (ER) and anterograde trafficking through the secretory pathway. N-Glycans are attached to nascent polypeptides at consensus sites, N-X-T/S (X ≠ P), by one of two enzymatic isoforms of the oligosaccharyltransferase (OST), STT3A or STT3B. Here, we examined the effect of the consensus site X and hydroxyl residue on the distributions of co- and post-translational N-glycosylation of a type I transmembrane glycopeptide scaffold. Using rapid radioactive pulse-chase experiments to resolve co-translational (STT3A) and post-translational (STT3B) events, we determined that NXS consensus sites containing large hydrophobic and negatively charged middle residues are frequently skipped by STT3A during protein translation. Post-translational modification of the cotranslationally skipped sites by STT3B was similarly hindered by the middle X residue, resulting in hypoglycosylation of NXS sites containing large hydrophobic and negatively charged side chains. In contrast, NXT consensus sites (barring NWT) were efficiently modified by the cotranslational machinery, reducing STT3B's role in modifying consensus sites skipped during protein translation. A strong correlation between cotranslational N-glycosylation efficiency and the rate of post-translational N-glycosylation was determined, showing that the OST STT3A and STT3B isoforms are similarly influenced by the hydroxyl and middle X consensus site residues. Substituting various middle X residues into an OST eubacterial homologous structure revealed that small and polar consensus site X residues fit well in the peptide binding site whereas large hydrophobic and negatively charged residues were harder to accommodate, indicating conserved enzymatic mechanisms for the mammalian OST isoforms.
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