The mechanism of synthesis of the polysaccharide part of mannan in Saccharomyces cerevisiae
Saccharomyces cerevisiae wild-type and mutant cells affected in the structure of mannan outer chain were shown to possess in vivo one major dolichol-P-P-bound oligosaccharide. The size, monosaccharide composition, and pattern obtained upon acetolysis and paper chromatography of the oligosaccharide w...
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1981
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v210_n1_p372_Parodi http://hdl.handle.net/20.500.12110/paper_00039861_v210_n1_p372_Parodi |
| Aporte de: |
| Sumario: | Saccharomyces cerevisiae wild-type and mutant cells affected in the structure of mannan outer chain were shown to possess in vivo one major dolichol-P-P-bound oligosaccharide. The size, monosaccharide composition, and pattern obtained upon acetolysis and paper chromatography of the oligosaccharide were the same for all strains and for the main corresponding compound isolated from animal tissues. Evidence is presented indicating that the dolichol-P-P derivative occurring in vivo, and containing 2-N-acetylglucosamine, 9-mannose, and 3-glucose residues, is the intermediate involved in yeast protein glycosylation. The transfer of the oligosaccharide to protein was followed in vivo by the excision of the glucose and at the most one mannose residue. Mannoses were then added to the trimmed saccharide moiety. No difference between the first stages (i.e., excision of monosaccharides) of the processing of the protein-bound oligosaccharides by wild-type and mutant cells was found. However, mutants carrying the mnn 1 mutation, which are known to be devoid of terminal α(1-3)-linked mannose residues in the mannan outer chain and inner core, were found not to add such mannose residues to the already glucose-free protein-bound oligosaccharide. © 1981. |
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