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FEBS Lett. 1994 May 9;344(1):83-6.

The N-oligosaccharyltransferase complex from yeast.

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Lehrstuhl für Zellbiologie und Pflanzenphysiologie, Universität Regensburg, Germany.


N-Oligosaccharyltransferase catalyzes the N-glycosylation of asparagine residues of nascent polypeptide chains in the endoplasmic reticulum, a pathway highly conserved in all eukaryotes. An enzymatically active complex was isolated from microsomal membranes from Saccharomyces cerevisiae, which is composed of four proteins: Wbp1p and Swp1p (previously found to be encoded by two essential genes necessary for N-glycosylation in vivo and in vitro) and two additional proteins with a molecular mass of 60/62 kDa and 34 kDa. The 60/62 component represents differentially glycosylated forms of a protein that has sequence homology to ribophorin I. Wbp1p and Swp1p reveal homology to mammalian OST 48 and ribophorin II, respectively. Ribophorin I and II and OST 48 were recently shown to be constituents of the mammalian transferase from dog pancreas. The data reveal a high conservation of the organization of this enzyme activity.

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