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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Autor principal: Parodi, A.J.
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00039861_v210_n1_p372_Parodi
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spelling todo:paper_00039861_v210_n1_p372_Parodi2023-10-03T13:56:55Z The mechanism of synthesis of the polysaccharide part of mannan in Saccharomyces cerevisiae Parodi, A.J. dolichol diphosphate dolichol phosphate mannan oligosaccharide polysaccharide protein animal article biosynthesis chemistry chicken comparative study female in vitro study metabolism oviduct protein binding Saccharomyces cerevisiae Animal Chemistry Chickens Comparative Study Dolichol Phosphates Female In Vitro Mannans Oligosaccharides Oviducts Polysaccharides Protein Binding Proteins 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 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00039861_v210_n1_p372_Parodi
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic dolichol diphosphate
dolichol phosphate
mannan
oligosaccharide
polysaccharide
protein
animal
article
biosynthesis
chemistry
chicken
comparative study
female
in vitro study
metabolism
oviduct
protein binding
Saccharomyces cerevisiae
Animal
Chemistry
Chickens
Comparative Study
Dolichol Phosphates
Female
In Vitro
Mannans
Oligosaccharides
Oviducts
Polysaccharides
Protein Binding
Proteins
Saccharomyces cerevisiae
spellingShingle dolichol diphosphate
dolichol phosphate
mannan
oligosaccharide
polysaccharide
protein
animal
article
biosynthesis
chemistry
chicken
comparative study
female
in vitro study
metabolism
oviduct
protein binding
Saccharomyces cerevisiae
Animal
Chemistry
Chickens
Comparative Study
Dolichol Phosphates
Female
In Vitro
Mannans
Oligosaccharides
Oviducts
Polysaccharides
Protein Binding
Proteins
Saccharomyces cerevisiae
Parodi, A.J.
The mechanism of synthesis of the polysaccharide part of mannan in Saccharomyces cerevisiae
topic_facet dolichol diphosphate
dolichol phosphate
mannan
oligosaccharide
polysaccharide
protein
animal
article
biosynthesis
chemistry
chicken
comparative study
female
in vitro study
metabolism
oviduct
protein binding
Saccharomyces cerevisiae
Animal
Chemistry
Chickens
Comparative Study
Dolichol Phosphates
Female
In Vitro
Mannans
Oligosaccharides
Oviducts
Polysaccharides
Protein Binding
Proteins
Saccharomyces cerevisiae
description 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.
format JOUR
author Parodi, A.J.
author_facet Parodi, A.J.
author_sort Parodi, A.J.
title The mechanism of synthesis of the polysaccharide part of mannan in Saccharomyces cerevisiae
title_short The mechanism of synthesis of the polysaccharide part of mannan in Saccharomyces cerevisiae
title_full The mechanism of synthesis of the polysaccharide part of mannan in Saccharomyces cerevisiae
title_fullStr The mechanism of synthesis of the polysaccharide part of mannan in Saccharomyces cerevisiae
title_full_unstemmed The mechanism of synthesis of the polysaccharide part of mannan in Saccharomyces cerevisiae
title_sort mechanism of synthesis of the polysaccharide part of mannan in saccharomyces cerevisiae
url http://hdl.handle.net/20.500.12110/paper_00039861_v210_n1_p372_Parodi
work_keys_str_mv AT parodiaj themechanismofsynthesisofthepolysaccharidepartofmannaninsaccharomycescerevisiae
AT parodiaj mechanismofsynthesisofthepolysaccharidepartofmannaninsaccharomycescerevisiae
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