Ablation of N-acetylglucosaminyltransferases in Caenorhabditis induces expression of unusual intersected and bisected N-glycans
| Autor: | Shi Yan, Huijie Wang, Iain B. H. Wilson, Harry Schachter, Chunsheng Jin, Katharina Paschinger |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Glycan Glycosylation animal structures Mutant Biophysics Mannose N-Acetylglucosaminyltransferases Biochemistry Article Animals Genetically Modified Glycomics 03 medical and health sciences symbols.namesake chemistry.chemical_compound Polysaccharides Exoglycosidase Animals Caenorhabditis elegans Caenorhabditis elegans Proteins Molecular Biology Gene integumentary system 030102 biochemistry & molecular biology biology Chemistry Golgi apparatus biology.organism_classification Cell biology carbohydrates (lipids) Caenorhabditis 030104 developmental biology Mutation symbols biology.protein |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - General Subjects. 1862:2191-2203 |
| ISSN: | 0304-4165 |
| DOI: | 10.1016/j.bbagen.2018.07.002 |
| Popis: | The modification in the Golgi of N-glycans by N-acetylglucosaminyltransferase I (GlcNAc-TI, MGAT1) can be considered to be a hallmark of multicellular eukaryotes as it is found in all metazoans and plants, but rarely in unicellular organisms. The enzyme is key for the normal processing of N-glycans to either complex or paucimannosidic forms, both of which are found in the model nematode Caenorhabditis elegans. Unusually, this organism has three different GlcNAc-TI genes (gly-12, gly-13 and gly-14); therefore, a complete abolition of GlcNAc-TI activity required the generation of a triple knock-out strain. Previously, the compositions of N-glycans from this mutant were described, but no detailed structures. Using an off-line HPLC-MALDI-TOF-MS approach combined with exoglycosidase digestions and MS/MS, we reveal that the multiple hexose residues of the N-glycans of the gly-12;gly-13;gly-14 triple mutant are not just mannose, but include galactoses in three different positions (β-intersecting, β-bisecting and α-terminal) on isomeric forms of Hex(4-8)HexNAc(2) structures; some of these structures are fucosylated and/or methylated. Thus, the N-glycomic repertoire of Caenorhabditis is even wider than expected and exhibits a large degree of plasticity even in the absence of key glycan processing enzymes from the Golgi apparatus. |
| Databáze: | OpenAIRE |
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