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J. Biol. Chem., Vol. 281, Issue 48, 36742-36751, December 1, 2006

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Identification and Characterization of a1,3-Glucosyltransferase That Synthesizes the Glc-1,3-Fuc Disaccharide on Thrombospondin Type 1 Repeats^*

Krisztina Kozma, Jeremy J. Keusch, Björn Hegemann¹, Kelvin B. Luther, Dominique Klein, Daniel Hess, Robert S. Haltiwanger, and Jan Hofsteenge²

From the Friedrich Miescher Institute, Maulbeerstrasse 66, CH-4058 Basel, Switzerland and Department of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, Stony Brook University, Stony Brook, New York 11794-5215

Thrombospondin type 1 repeats (TSRs) are biologically important domains of extracellular proteins. They are modified with a unique Glc1,3Fuc1-O-linked disaccharide on either serine or threonine residues. Here we identify the putative glycosyltransferase, B3GTL, as the 1,3-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 1,3-N-acetylglucosaminyltransferase that modifies O-linked fucosyl residues in proteins containing epidermal growth factor-like domains, such as Notch. 1,3-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 1,3-linkage to the fucose in TSR. The activity profiles of 1,3-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 1,3-glucosyltransferase gene allows us to manipulate the formation of the rare Glc1,3Fuc1 structure to investigate its biological function.

Received for publication, June 20, 2006 , and in revised form, September 6, 2006.

^* This work was supported in part by National Institutes of Health Grant GM61126. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Present address: Research Institute of Molecular Pathology, Dr. Bohr-Gasse 7, 1030 Vienna, Austria.

² To whom correspondence should be addressed. Tel.: 41-61-6974722; Fax: 41-61-6973976; E-mail: jan.hofsteenge{at}fmi.ch.

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