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J. Biol. Chem., Vol. 255, Issue 14, 6713-6716, 07, 1980

Synthesis of N- and O-linked glycopeptides in oviduct membrane preparations

JA Hanover, WJ Lennarz and JD Young

A hen oviduct membrane preparation that catalyzes both the N- and O- glycosylation of exogenous acceptor peptides was used to examine the possible involvement of lipid intermediates in enzymatic O- glycosylation. The results indicate that, under a variety of experimental conditions in which the dolichol-linked saccharides involved in N-glycosylation are readily observed, no lipid-linked intermediates for O-glycosylation could be detected. Whereas N- glycosylation is abolished by tunicamycin treatment and stimulated by dolichol phosphate addition, O-glycosylation is unaffected by such treatments. Further, the results of subcellular fractionation of oviduct membranes suggest that N-acetylgalactosaminyl:polypeptide transferase is localized primarily in membranes derived from the smooth endoplasmic reticulum and Golgi apparatus. This is in contrast to the subcellular site of N-glycosylation, which has previously been shown to be primarily the rough endoplasmic reticulum. These findings are discussed in relation to the function of dolichol phosphate in protein glycosylation.
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