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• W1965654564 abstract "Primary structural requirements both for N- and O-glycosylation have been studied using a series of synthetic peptides and a membrane fraction from Saccharomyces cerevisiae. N-Glycosylation: the tripeptide sequence Asn-Xaa-Thr/Ser was found to be necessary for the transfer of saccharide units from oligosaccharide-lipid to asparagine. Substitution of asparagine by aspartic acid or glutamine, or replacement of threonine by valine in the hexapeptide Tyr-Asn-Leu-Thr-Ser-Val prevents its glycosylation. Also, a proline residue in the position of Xaa makes the peptide unable to function as an acceptor. Transfer onto asparagine occurs only efficiently if both the α-amino group of asparagine and the α-carboxyl moiety of the hydroxy amino acid are blocked. Yield of glycosylation improves with increasing peptide chain length. With regard to the glycosyl donor dolichyl diphosphate-bound GlcNAc2Man9Glc3 is the preferred substrate. Non-glucosylated glycolipid Dol-PP-GlcNAc2Man9 is a poor donor, whereas smaller precursors Dol-PP-GlcNAc2 and Dol-PP-GlcNAc2Man1 allow reasonable transfer. O-Glycosylation: no marker sequence can be derived for the formation of an O-glycosidic linkage via Dol-P-Man. Introduction of a proline residue in vicinity to the hydroxy amino acid leads to a significant improvement of glycosyl transfer. It is postulated that accessibility of potential O-glycosylation sites rather than a specific sequence may be a prerequisite for O-glycosylation." @default.
• W1965654564 created "2016-06-24" @default.
• W1965654564 creator A5056736968 @default.
• W1965654564 creator A5078596439 @default.
• W1965654564 date "1984-06-29" @default.
• W1965654564 modified "2023-09-26" @default.
• W1965654564 title "Primary structural requirements for N- and O-glycosylation of yeast mannoproteins" @default.
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• W1965654564 doi "https://doi.org/10.1016/0304-4165(84)90267-8" @default.
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