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Volume 270, Number 13, Issue of March 31, 1995 pp. 7281-7287
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Characterization and Partial Purification of a Novel Enzymatic Activity
UDP-GlcNAc:Ser-PROTEIN N-ACETYLGLUCOSAMINE-1-PHOSPHOTRANSFERASE FROM THE CELLULAR SLIME MOLD DICTYOSTELIUM DISCOIDEUM

(Received for publication, November 14, 1994; and in revised form, January 3, 1995)

Silvana Merello,  Armando J. Parodi ,  Roberto Couso

An enzymatic activity that transfers N-acetylglucosamine-1-phosphate residues from UDP-GlcNAc to serine units in proteins (UDP-GlcNAc:Ser-protein N-acetylglucosamine-1-phosphotransferase) was detected in membranes of the cellular slime mold Dictyostelium discoideum. The enzyme was partially purified by affinity chromatography in concanavalin A-Sepharose and ion exchange chromatography in a Mono Q column. The enzyme showed an absolute requirement for bivalent cations, Mn being more effective than Mg. It had a broad optimum pH value (6.5-9.0). The K for UDP-GlcNAc was 18 µM. In cell free assays it used apomucin and native or 8 M urea-denatured thyroglobulin but neither bovine serum albumin nor native or denatured uteroferrin as exogenous acceptors. Analysis of proteins isolated from cells grown in the presence of [P]phosphate and from the culture medium showed that the majority of proteins bearing the structure GlcNAc-1-P-Ser were secreted. In equilibrium density centrifugations of microsomes, the enzyme appeared in membranes having lighter densities than the enzyme that phosphorylates high mannose-type oligosaccharides. This showed that the activity that phosphorylates serine residues in proteins (UDP-GlcNAc:Ser-protein N-acetylglucosamine-1-phosphotransferase) is different from that phosphorylating protein-linked high mannose-type oligosaccharides (UDP-GlcNAc:glycoprotein N-acetylglucosamine-1-phosphotransferase).



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