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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


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.

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:26 Aug 2016 07:32
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:10.1074/jbc.M109.058354
PubMed ID:19858195
Permanent URL: http://doi.org/10.5167/uzh-25754

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