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Gewählte Publikation:

Titz, A; Butschi, A; Henrissat, B; Fan, YY; Hennet, T; Razzazi-Fazeli, E; Hengartner, MO; Wilson, IB; Künzler, M; Aebi, M.
(2009): 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.
J Biol Chem. 2009; 284(52):36223-36233 FullText FullText_BOKU

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 beta 1,4-galactoside linked to the alpha 1,6-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 alpha 1,6-linked N-glycan core fucosides and required Golgi-dependent modifications on the oligosaccharide antennae for optimal synthesis of the Gal-beta 1,4-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.
Autor*innen der BOKU Wien:
Wilson Iain B.H.
Find related publications in this database (using NML MeSH Indexing)
Animals -
Caenorhabditis elegans - enzymology
Fucose - genetics
Galactosyltransferases - genetics
Mutation -
Oligosaccharides - biosynthesis
Phylogeny -
Recombinant Proteins - genetics
Substrate Specificity - physiology

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