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J Biol Chem, Vol. 274, Issue 33, 22915-22918, August 13, 1999

COMMUNICATION
Human Homolog of Caenorhabditis elegans sqv-3 Gene Is Galactosyltransferase I Involved in the Biosynthesis of the Glycosaminoglycan-Protein Linkage Region of Proteoglycans

Tetsuya Okajima, Kumi Yoshida^§, Tadao Kondo^¶, and Koichi Furukawa

From the  Department of Biochemistry II, Nagoya University School of Medicine, Tsurumai, Nagoya 466-0065, the ^§ School of Life Studies, Sugiyama Jogakuen University, Chikusa, Nagoya 464-0802, and the ^¶ Chemical Instrument Center, Nagoya University, Chikusa, Nagoya 464-8602, Japan

A cDNA encoding a novel galactosyltransferase was identified based on BLAST analysis of expressed sequence tags, and the cDNA clones were isolated from a human melanoma line library. The new cDNA sequence encoded a type II membrane protein with 327 amino acid sequence and showed 38% homology to the Caenorhabditis elegans sqv-3 gene involved in the vulval invagination and oocyte development. Extracts from L cells transfected with the galactosyltransferase cDNA in an expression vector and a fusion protein with protein A exhibited marked galactosyltransferase activity specific for p-nitrophenyl--D-xylopyranoside. Moreover, transfection with the cloned cDNA restored glycosaminoglycan synthesis of galactosyltransferase I-deficient Chinese hamster ovary mutant pgsB-761 cells. Analysis of the enzyme product by -galactosidase digestion, mass spectroscopy, and NMR spectroscopy revealed that the reaction product was formed via -1,4 linkage, indicating that the enzyme is galactosyltransferase I (UDP-galactose:O--D-xylosylprotein 4--D-galactosyltransferase, EC 2.4.1.133) involved in the synthesis of the glycosaminoglycan-protein linkage region of proteoglycans.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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