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J Biol Chem ; 281(48): 36742-51, 2006 Dec 01.
Article in English | MEDLINE | ID: mdl-17032646

ABSTRACT

Thrombospondin type 1 repeats (TSRs) are biologically important domains of extracellular proteins. They are modified with a unique Glcbeta1,3Fucalpha1-O-linked disaccharide on either serine or threonine residues. Here we identify the putative glycosyltransferase, B3GTL, as the beta1,3-glucosyltransferase involved in the biosynthesis of this disaccharide. This enzyme is conserved from Caenorhabditis elegans to man and shares 28% sequence identity with Fringe, the beta1,3-N-acetylglucosaminyltransferase that modifies O-linked fucosyl residues in proteins containing epidermal growth factor-like domains, such as Notch. beta1,3-Glucosyltransferase glucosylates properly folded TSR-fucose but not fucosylated epidermal growth factor-like domain or the non-fucosylated modules. Specifically, the glucose is added in a beta1,3-linkage to the fucose in TSR. The activity profiles of beta1,3-glucosyltransferase and protein O-fucosyltransferase 2, the enzyme that carries out the first step in TSR O-fucosylation, superimpose in endoplasmic reticulum subfractions obtained by density gradient centrifugation. Both enzymes are soluble proteins that efficiently modify properly folded TSR modules. The identification of the beta1,3-glucosyltransferase gene allows us to manipulate the formation of the rare Glcbeta1,3Fucalpha1 structure to investigate its biological function.


Subject(s)
Disaccharides/chemistry , Glucosyltransferases/chemistry , Thrombospondins/chemistry , Animals , Caenorhabditis elegans , Centrifugation, Density Gradient , Endoplasmic Reticulum/metabolism , Epidermal Growth Factor/chemistry , Fucose/chemistry , Glucosyltransferases/metabolism , Humans , Peptides/chemistry , Rats , Spectrometry, Mass, Electrospray Ionization , Substrate Specificity
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