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Vol. 273, Issue 1, 58-65, January 2, 1998

Genomic Cloning and Expression of Three Murine UDP-galactose: beta -N-Acetylglucosamine beta 1,3-Galactosyltransferase Genes

Thierry HennetDagger , André DinterDagger , Peter Kuhnert, Taj S. Mattupar , Pauline M. Ruddpar , and Eric G. BergerDagger

From the Dagger  Institute of Physiology, University of Zurich, 8057 Zurich, Switzerland, the  Institute of Veterinary Bacteriology, University of Berne, 3012 Berne, Switzerland, and the par  Glycobiology Institute, Department of Biochemistry, Oxford University, Oxford OX1 3QU, United Kingdom

Based on the detection of expressed sequence tags that are similar to known galactosyltransferase sequences, we have isolated three novel UDP-galactose:beta -N-acetylglucosamine beta 1,3-galactosyltransferase (beta 3GalT) genes from a mouse genomic library. The three genes, named beta 3GalT-I, -II, and -III, encode type II transmembrane proteins of 326, 422, and 331 amino acids, respectively. The three proteins constitute a distinct subfamily as they do not share any sequence identity with other eucaryotic galactosyltransferases. Also, the entire protein-coding region of the three beta 3GalT genes was contained in a single exon, which contrasts with the genomic organization of the beta 1,4- and alpha 1,3-galactosyltransferase genes. The three beta 3GalT genes were mainly expressed in brain tissue. The expression of the full-length murine genes as recombinant baculoviruses in insect cells revealed that the beta 3GalT enzymes share the same acceptor specificity for beta -linked GlcNAc, although they differ in their Km for this acceptor and the donor UDP-Gal. The identification of beta 3GalT genes emphasizes the structural diversity present in the galactosyltransferase gene family.


Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.



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