Molecular Basis for Galactosylation of Core Fucose Residues in Invertebrates
Identification of Caenorhabditis Elegans N-Glycan Core α1,6-Fucoside β1,4-Galactosyltransferase Galt-1 as a Member of a Novel Glycosyltransferase Family
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2009-12-25
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Journal Article
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yes
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Abstract
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 β1,4-galactoside linked to the α1,6-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 α1,6-linked N-glycan core fucosides and required Golgi- dependent modifications on the oligosaccharide antennae for optimal synthesis of the Gal-β1,4-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.
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published
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284 (52)
Pages / Article No.
36223 - 36233
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American Society for Biochemistry and Molecular Biology
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03408 - Aebi, Markus (emeritus) / Aebi, Markus (emeritus)