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Glycoprotein biosynthesis in yeast
Author(s) -
Herscovics Annette,
Orlean Peter
Publication year - 1993
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.7.6.8472892
Subject(s) - glycosylation , yeast , asparagine , biochemistry , saccharomyces cerevisiae , mutant , threonine , biosynthesis , biology , glycan , glycoprotein , n linked glycosylation , serine , gene , enzyme , chemistry
Many proteins in the yeast Saccharomyces cerevisiae are modified by the attachment of N‐linked saccharides to asparagine, of O ‐linked mannose glycans to serine or threonine, and of glycosylphosphoinositol membrane anchors. The biosynthetic events leading to these modifications are coupled to the secretory pathway. Early stages of N ‐linked glycosylation and the formation of glycosylphosphoinositol anchors have been conserved through evolution of eukaryotes. Studies of yeast offer a variety of genetic and molecular biological approaches, which have led to the isolation of different glycosylation mutants and of genes for enzymes involved in glycosylation. Yeast mutants are useful to identify biosynthetic intermediates, to establish whether a given enzyme is essential for viability, and to determine how cellular functions are affected when glycosylation is perturbed. Yeast glycosylation mutants and genes can be used to identify their counterparts in other eukaryotes.—Herscovics, A.; Orlean, P. Glycoprotein biosynthesis in yeast. FASEB J. 7 : 540‐550; 1993.