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Ablation of N-acetylglucosaminyltransferases in Caenorhabditis induces expression of unusual intersected and bisected N-glycans

Journal article
Authors S. Yan
H. Wang
H. Schachter
Chunsheng Jin
I. B. H. Wilson
K. Paschinger
Published in Biochimica et Biophysica Acta - General Subjects
Volume 1862
Issue 10
Pages 2191-2203
ISSN 0304-4165
Publication year 2018
Published at Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 2191-2203
Language en
Links dx.doi.org/10.1016/j.bbagen.2018.07...
Keywords GlycomicsN-glycansNematode
Subject categories Biochemistry

Abstract

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 Hex4-8HexNAc2 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.

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