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Type of publication: Journal Article
Type of document: Full Paper

Year: 2009

Authors: Titz, A; Butschi, A; Henrissat, B; Fan, YY; Hennet, T; Razzazi-Fazeli, E; Hengartner, MO; Wilson, IB; K├╝nzler, M; Aebi, M

Title: Molecular basis for galactosylation of core fucose residues in invertebrates: identification of caenorhabditis elegans N-glycan core alpha1,6-fucoside beta1,4-galactosyltransferase GALT-1 as a member of a novel glycosyltransferase family.

Source: J Biol Chem. 2009; 284(52):36223-36233

Authors Vetmeduni Vienna:

Razzazi-Fazeli Ebrahim

Vetmed Research Units

Galectin CGL2 from the ink cap mushroom Coprinopsis cinerea displays toxicity toward the model nematode Caenorhabditis elegans. A mutation in a putative glycosyltransferase-encoding gene resulted in a CGL2-resistant C. elegans strain characterized by N-glycans lacking the beta1,4-galactoside linked to the alpha1,6-linked core fucose. Expression of the corresponding GALT-1 protein in insect cells was used to demonstrate a manganese-dependent galactosyltransferase activity. In vitro, the GALT-1 enzyme showed strong selectivity for acceptors with alpha1,6-linked N-glycan core fucosides and required Golgi- dependent modifications on the oligosaccharide antennae for optimal synthesis of the Gal-beta1,4-fucose structure. Phylogenetic analysis of the GALT-1 protein sequence identified a novel glycosyltransferase family (GT92) with members widespread among eukarya but absent in mammals.

Keywords Pubmed: Animals
Caenorhabditis elegans/enzymology*
Caenorhabditis elegans/genetics
Recombinant Proteins/genetics
Recombinant Proteins/metabolism
Substrate Specificity/physiology

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