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 Dec 25;284(52):36223-36233. doi: 10.1074/jbc.M109.058354. Epub 2009 Oct 26.

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 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Caenorhabditis elegans / enzymology*
  • Caenorhabditis elegans / genetics
  • Fucose / genetics
  • Fucose / metabolism
  • Galactosyltransferases / genetics
  • Galactosyltransferases / metabolism*
  • Mutation
  • Oligosaccharides / biosynthesis*
  • Oligosaccharides / genetics
  • Phylogeny*
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Substrate Specificity / physiology

Substances

  • Oligosaccharides
  • Recombinant Proteins
  • Fucose
  • Galactosyltransferases