ArticleThe Journal of biological chemistry2012
Identification of novel α1,3-galactosyltransferase and elimination of α-galactose-containing glycans by disruption of multiple α-galactosyltransferase genes in Schizosaccharomyces pombe.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 23 citations in OpenAlex.
- Integrative glycomic analysis reveals the crucial role of protein glycosylation in fungal pathogenesis.PLoS pathogens · 2025Article
- Elevated levels of sphingolipid MIPC in the plasma membrane disrupt the coordination of cell growth with cell wall formation in fission yeast.PLoS genetics · 2023Article
- Exploring the Ecological Implications of Microbiota Diversity in Birds: Natural Barriers Against Avian Malaria.Frontiers in immunology · 2022Article
- Anti-Tick Microbiota Vaccine ImpactsVaccines · 2020Article
- Tick galactosyltransferases are involved in α-Gal synthesis and play a role during Anaplasma phagocytophilum infection and Ixodes scapularis tick vector development.Scientific reports · 2018Article
- Diversity of Cell Wall Related Proteins in Human Pathogenic Fungi.Journal of fungi (Basel, Switzerland) · 2017Article
- More Than Just Oligomannose: An N-glycomic Comparison of Penicillium Species.Molecular & cellular proteomics : MCP · 2016Article
- Engineering yeast for producing human glycoproteins: where are we now?Future microbiology · 2015Article
- Characterization of genome-reduced fission yeast strains.Nucleic acids research · 2013Article
- TheFood technology and biotechnologyArticle
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3 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The oligosaccharides from fission yeast Schizosaccharomyces pombe contain large amounts of D-galactose (Gal) in addition to D-mannose (Man), in contrast to the budding yeast Saccharomyces cerevisiae. Detailed structural analysis has revealed that the Gal residues are attached to the N- and O-linked oligosaccharides via α1,2- or α1,3-linkages. Previously we constructed and characterized a septuple α-galactosyltransferase disruptant (7GalTΔ) anticipating a complete lack of α-Gal residues. However, the 7GalTΔ strain still contained oligosaccharides consisting of α1,3-linked Gal residues, indicating the presence of at least one more additional unidentified α1,3-galactosyltransferase. In this study we searched for unidentified putative glycosyltransferases in the S. pombe genome sequence and identified three novel genes, named otg1(+)-otg3(+) (α one, three-galactosyltransferase), that belong to glycosyltransferase gene family 8 in the Carbohydrate Active EnZymes (CAZY) database. Gal-recognizing lectin blotting and HPLC analyses of pyridylaminated oligosaccharides after deletion of these three additional genes from 7GalTΔ strain demonstrated that the resultant disruptant missing 10 α-galactosyltransferase genes, 10GalTΔ, exhibited a complete loss of galactosylation. In an in vitro galactosylation assay, the otg2(+) gene product had Gal transfer activity toward a pyridylaminated Man(9)GlcNAc(2) oligosaccharide and pyridylaminated Manα1,2-Manα1,2-Man oligosaccharide. In addition, the otg3(+) gene product exhibited Gal transfer activity toward the pyridylaminated Man(9)GlcNAc(2) oligosaccharide. Generation of an α1,3-linkage was confirmed by HPLC analysis, α-galactosidase digestion analysis, (1)H NMR spectroscopy, and LC-MS/MS analysis. These results indicate that Otg2p and Otg3p are involved in α1,3-galactosylation of S. pombe oligosaccharides.
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