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J. Biol. Chem., Vol. 283, Issue 4, 1985-1991, January 25, 2008

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A Necessary and Sufficient Determinant for Protein-selective Glycosylation in Vivo^*

From the Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, Missouri 63110

A limited number of glycoproteins including luteinizing hormone and carbonic anhydrase-VI (CA6) bear N-linked oligosaccharides that are modified with β1,4-linked N-acetylgalactosamine (GalNAc). The selective addition of GalNAc to these glycoproteins requires that the β1,4-N-acetylgalactosaminyltransferase (βGT) recognize both the oligosaccharide acceptor and a peptide recognition determinant on the substrate glycoprotein. We report here that two recently cloned βGTs, βGT3 and βGT4, that are able to transfer GalNAc to GlcNAc in β1,4-linkage display the necessary glycoprotein specificity in vivo. Both βGTs transfer GalNAc to N-linked oligosaccharides on the luteinizing hormone subunit and CA6 but not to those on transferrin (Trf). A single peptide recognition determinant encoded in the carboxyl-terminal 19-amino acid sequence of bovine CA6 mediates transfer of GalNAc to each of its two N-linked oligosaccharides. The addition of this 19-amino acid sequence to the carboxyl terminus of Trf confers full acceptor activity onto Trf for both βGT3 and βGT4 in vivo. The complete 19-amino acid sequence is required for optimal GalNAc addition in vivo, indicating that the peptide sequence is both necessary and sufficient for recognition by βGT3 and βGT4.

Received for publication, October 2, 2007 , and in revised form, November 28, 2007.

^* This work was supported by National Institutes of Health Grant R01DK41738 (to J. U. B.). 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: Graduate School of Biomedical Sciences, University of Texas Health Science Center San Antonio, 7703 Floyd Curl Dr., MC 7819, San Antonio, TX 78229-3900.

² Present address: Transkaryotic Therapies, Inc.,700 Main St., Cambridge, MA 02139.

³ To whom correspondence should be addressed: Washington University School of Medicine, Dept. of Pathology and Immunology, 4940 Parkview Place, St. Louis, MO 63110. Fax: 314-362-8888; E-mail: Baenziger{at}wustl.edu.

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