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J. Biol. Chem., Vol. 279, Issue 38, 40035-40043, September 17, 2004

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The Stem Region of the Sulfotransferase GlcNAc6ST-1 Is a Determinant of Substrate Specificity^*

Christopher L. de Graffenried and Carolyn R. Bertozzi¶||**

From the Departments of Chemistry and ^¶Molecular and Cell Biology and ^||Howard Hughes Medical Institute, University of California, Berkeley, California 94720

The GlcNAc-6-sulfotransferases are a family of Golgi-resident enzymes that modulate glycan function. Two members of this family, GlcNAc6ST-1 and -2, collaborate in the biosynthesis of ligands for the leukocyte adhesion molecule L-selectin. Although their biochemical properties are similar in vitro, the enzymes have distinct glycoprotein substrate preferences in vivo. The sulfotransferases share similar overall architecture with the exception of an extended stem region in GlcNAc6ST-1 that is absent in GlcNAc6ST-2. In this study we probed the importance of the stem region with respect to substrate preference, localization, and oligomerization. Analysis of truncation mutants demonstrated that perturbation of the stem region of GlcNAc6ST-1 affects the cellular substrate preference of the enzyme without altering its retention within the Golgi. A chimeric enzyme comprising the stem region of GlcNAc6ST-1 inserted between the catalytic and transmembrane domains of GlcNAc6ST-2 had the same substrate preference as native GlcNAc6ST-1. In cells, GlcNAc6ST-1 exists as a dimer; two cysteine residues within the stem and transmembrane domain were found to be critical for dimerization. However, disruption of the dimer by mutagenesis did not affect either localization or substrate preference. Collectively, these results indicate that the stem region of GlcNAc6ST-1 influences substrate specificity, independent of its role in dimerization or Golgi retention.

Received for publication, May 24, 2004 , and in revised form, June 25, 2004.

^* This work was supported in part by National Institutes of Health Grant GM59907. 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.

Supported by a National Science Foundation Predoctoral Fellowship.

^** To whom correspondence should be addressed. Tel.: 510-643-1682; Fax: 510-643-2628; E-mail: crb{at}berkeley.edu.

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