ArticleThe Biochemical journal2003
Free-oligosaccharide control in the yeast Saccharomyces cerevisiae: roles for peptide:N-glycanase (Png1p) and vacuolar mannosidase (Ams1p).
Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 59 citations in OpenAlex.
- Structural mechanism of protein recognition by the FW domain of autophagy receptor Nbr1.Nature communications · 2022Article
- Cryo-EM structure of fission yeast tetrameric α-mannosidase Ams1.FEBS open bio · 2020Article
- First Proteomic Approach to Identify Cell Death Biomarkers in Wine Yeasts during Sparkling Wine Production.Microorganisms · 2019Article
- Free glycans derived fromThe Journal of biological chemistry · 2019Article
- Review
- Article
- Generation and degradation of free asparagine-linked glycans.Cellular and molecular life sciences : CMLS · 2015Review
- Eukaryotic oligosaccharyltransferase generates free oligosaccharides during N-glycosylation.The Journal of biological chemistry · 2013Article
- Dissociation of the H3K36 demethylase Rph1 from chromatin mediates derepression of environmental stress-response genes under genotoxic stress in Saccharomyces cerevisiae.Molecular biology of the cell · 2013Article
- Protein Glycosylation in Aspergillus fumigatus Is Essential for Cell Wall Synthesis and Serves as a Promising Model of Multicellular Eukaryotic Development.International journal of microbiology · 2012Article
- Endoplasmic reticulum-associated degradation (ERAD) and free oligosaccharide generation in Saccharomyces cerevisiae.The Journal of biological chemistry · 2011Article
- Article
- Evidence for an essential deglycosylation-independent activity of PNGase in Drosophila melanogaster.PloS one · 2010Article
- Free oligosaccharides to monitor glycoprotein endoplasmic reticulum-associated degradation in Saccharomyces cerevisiae.The Journal of biological chemistry · 2010Article
- Crystallization of Saccharomyces cerevisiae alpha-mannosidase, a cargo protein of the Cvt pathway.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
- Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum.The Journal of cell biology · 2009Article
- Kex2 protease converts the endoplasmic reticulum alpha1,2-mannosidase of Candida albicans into a soluble cytosolic form.Microbiology (Reading, England) · 2008Article
- Man2C1, an alpha-mannosidase, is involved in the trimming of free oligosaccharides in the cytosol.The Biochemical journal · 2006Article
- Free N-linked oligosaccharide chains: formation and degradation.Glycoconjugate journal · 2006Review
- Processing of N-linked glycans during endoplasmic-reticulum-associated degradation of a short-lived variant of ribophorin I.The Biochemical journal · 2003Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Free oligosaccharides (fOS) are generated during glycoprotein biosynthesis in mammalian cells. Here we report on the origin and fate of these structures in the yeast Saccharomyces cerevisiae. After metabolic radiolabelling with [2-(3)H]mannose ([2-(3)H]Man) for 30 min, Man(8)GlcNAc(2) was identified as the predominant fOS in this organism, and radioactivity associated with this structure was found to correspond to approximately 1% of that associated with the same structure N -linked to glycoprotein. Despite provoking a fourfold increase in radioactivity associated with lipid-linked oligosaccharide, the protein-synthesis inhibitor cycloheximide blocked [2-(3)H]Man incorporation into both endo-beta-D- N -acetylglucosamine H-sensitive N-glycans and fOS. Peptide:N-glycanase, encoded by the PNG1 gene, was found to be required for the generation of a large proportion of yeast fOS during, and soon after, protein glycosylation. Use of an ams1 Delta strain deficient in the vacuolar alpha-mannosidase revealed this enzyme to be responsible for the slow growth-associated catabolism of fOS. The present paper constitutes the first description of fOS formation in intact S. cerevisiae, and, with the demonstration that fOS are degraded by the vacuolar mannosidase, a novel function for this poorly understood enzyme has been identified.
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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.