ArticleThe Journal of biological chemistry2009
Biochemical characterization and membrane topology of Alg2 from Saccharomyces cerevisiae as a bifunctional alpha1,3- and 1,6-mannosyltransferase involved in lipid-linked oligosaccharide biosynthesis.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 39 citations in OpenAlex.
- FcLRR1 Regulates Hyphal Growth and Plant Infection inJournal of fungi (Basel, Switzerland) · 2026Article
- Clinical and genetic characterization of congenital disorders of glycosylation in 20 Chinese patients.Orphanet journal of rare diseases · 2025Article
- Functions ofJournal of fungi (Basel, Switzerland) · 2025Review
- Improving recombinant protein secretion inMetabolic engineering communications · 2025Article
- Topological and enzymatic analysis of human Alg2 mannosyltransferase reveals its role in lipid-linked oligosaccharide biosynthetic pathway.Communications biology · 2022Article
- Quantitative Proteome Profiling Reveals Cellobiose-Dependent Protein Processing and Export Pathways for the Lignocellulolytic Response in Neurospora crassa.Applied and environmental microbiology · 2020Article
- Processivity in Bacterial Glycosyltransferases.ACS chemical biology · 2020Review
- Reconstitution of the lipid-linked oligosaccharide pathway for assembly of high-mannose N-glycans.Nature communications · 2019Article
- Chemo-enzymatic synthesis of lipid-linked GlcNAc2Man5 oligosaccharides using recombinant Alg1, Alg2 and Alg11 proteins.Glycobiology · 2017Article
- New insight into the catalytic properties of rice sucrose synthase.Plant molecular biology · 2016Article
- Metabolically programmed quality control system for dolichol-linked oligosaccharides.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- N-linked protein glycosylation in the endoplasmic reticulum.Cold Spring Harbor perspectives in biology · 2013Review
- Domain organization of the polymerizing mannosyltransferases involved in synthesis of the Escherichia coli O8 and O9a lipopolysaccharide O-antigens.The Journal of biological chemistry · 2012Article
- Review
- 5-thiomannosides block the biosynthesis of dolichol-linked oligosaccharides and mimic class I congenital disorders of glycosylation.Chembiochem : a European journal of chemical biology · 2012Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
N-Linked glycosylation involves the ordered, stepwise synthesis of the unique lipid-linked oligosaccharide precursor Glc(3)Man(9) GlcNAc(2)-PP-Dol on the endoplasmic reticulum (ER), catalyzed by a series of glycosyltransferases. Here we characterize Alg2 as a bifunctional enzyme that is required for both the transfer of the alpha1,3- and the alpha1,6-mannose-linked residue from GDP-mannose to Man(1)GlcNAc(2)-PP-Dol forming the Man(3)GlcNAc(2)-PP-Dol intermediate on the cytosolic side of the ER. Alg2 has a calculated mass of 58 kDa and is predicted to contain four transmembrane-spanning helices, two at the N terminus and two at the C terminus. Contradictory to topology predictions, we prove that only the two N-terminal domains fulfill this criterion, whereas the C-terminal hydrophobic sequences contribute to ER localization in a nontransmembrane manner. Surprisingly, none of the four domains is essential for transferase activity because truncated Alg2 variants can exert their function as long as Alg2 is associated with the ER by either its N- or C-terminal hydrophobic regions. By site-directed mutagenesis we demonstrate that an EX(7)E motif, conserved in a variety of glycosyltransferases, is not important for Alg2 function in vivo and in vitro. Instead, we identify a conserved lysine residue, Lys(230), as being essential for activity, which could be involved in the binding of the phosphate of the glycosyl donor.
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