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Molecular basis for galactosylation of core fucose residues in invertebrates: Identification of Caenorhabditis elegans N-glycan core {alpha}1,6-fucoside {beta}1,4-galactosyltransferase GALT-1 as a member of a novel glycosyltransferase family - Zurich Open Repository and Archive


Titz, A; Butschi, A; Henrissat, B; Fan, Y Y; Hennet, T; Razzazi-Fazeli, E; Hengartner, M O; Wilson, I B H; Kuenzler, M; Aebi, M (2009). Molecular basis for galactosylation of core fucose residues in invertebrates: Identification of Caenorhabditis elegans N-glycan core {alpha}1,6-fucoside {beta}1,4-galactosyltransferase GALT-1 as a member of a novel glycosyltransferase family. Journal of Biological Chemistry, 284(52):36223-36233.

Abstract

Galectin CGL2 from the ink cap mushroom Coprinopsis cinerea displays toxicity towards 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 Galbeta1,4Fuc structure. Phylogenetic analysis of the GALT-1 protein sequence identified a novel glycosyltransferase family (GT92) with members widespread among eukarya but absent in mammals.

Abstract

Galectin CGL2 from the ink cap mushroom Coprinopsis cinerea displays toxicity towards 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 Galbeta1,4Fuc structure. Phylogenetic analysis of the GALT-1 protein sequence identified a novel glycosyltransferase family (GT92) with members widespread among eukarya but absent in mammals.

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Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Center for Integrative Human Physiology
07 Faculty of Science > Institute of Molecular Life Sciences
04 Faculty of Medicine > Institute of Physiology
07 Faculty of Science > Institute of Physiology
Dewey Decimal Classification:570 Life sciences; biology
610 Medicine & health
Language:English
Date:December 2009
Deposited On:16 Dec 2009 12:56
Last Modified:22 Jan 2017 06:14
Publisher:American Society for Biochemistry and Molecular Biology
ISSN:0021-9258
Additional Information:This research was originally published in Titz, A; Butschi, A; Henrissat, B; Fan, Y Y; Hennet, T; Razzazi-Fazeli, E; Hengartner, M O; Wilson, I B H; Kuenzler, M; Aebi, M (2009). Molecular basis for galactosylation of core fucose residues in invertebrates: Identification of Caenorhabditis elegans N-glycan core {alpha}1,6-fucoside {beta}1,4-galactosyltransferase GALT-1 as a member of a novel glycosyltransferase family. Journal of Biological Chemistry, 284(52):36223-36233. © the American Society for Biochemistry and Molecular Biology.
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:https://doi.org/10.1074/jbc.M109.058354
PubMed ID:19858195

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