Oligosaccharyltransferase Complex, Ribophorin-I, Ribophorin-II, OST48,and DAD1
Mammalian N-glycoproteins have been implicated as affecting a variety of biological processes such as cell growth, cell development, and cell communication, as well as protein stability and the control of protein folding (Varki et al. 1999). N-Glycan diversity arises from a common GlcNAc2-Man9-Glc3 precursor that is preassembled with dolichol-PP (Dol-PP), transferred en bloc to specific asparagine residues of the nascent polypeptide chain, and then remodeled by endoplasmic reticulum (ER)- and Golgi-resident α-glycosidases and glycosyltransferases (Kornfeld and Kornfeld 1985). Oligosaccharyltransferase (OST), a hetero-oligomeric protein complex associated with the ER membrane, occupies a central role in this pathway linking the Dol-PP- dependent reaction sequence of oligosaccharide precursor formation with the lipid- independent route of N-glycan processing and maturation.
KeywordsComplete Amino Acid Sequence Glycosyl Donor Glycosyl Acceptor Nascent Polypeptide Chain Hydroxyamino Acid
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- Aubert JP, Chiroutre M, Kerckaert JP, Helbecque N, Loucheux-Lefebvre MH (1982) Purification by affinity chromatography of the solubilized oligosaccharyltransferase from hen oviducts using a privileged secondary structure adopting peptide. Biochem Biophys Res Commun 104:1550–1559PubMedCrossRefGoogle Scholar
- Varki A, Cummings R, Esko J, Freeze H, Hart G, Marth J (1999) Essential of Glycobiology. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New YorkGoogle Scholar