Open AccessRole of glycosylation in the incorporation of intrinsic mannoproteins into cell walls of Saccharomyces cerevisiae
Author(s) -
Sanz Pascual,
Herrero Enrique,
Sentandreu Rafael
Publication year - 1989
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1989.tb03346.x
Subject(s) - tunicamycin , saccharomyces cerevisiae , glycosylation , mannose , biochemistry , yeast , mutant , glycoprotein , peptide , cell wall , n linked glycosylation , secretion , chemistry , glycan , biology , gene , unfolded protein response
Cell wall mannoproteins from Saccharomyces cerevisiae are completely or partially incorporated into their final location when N ‐glycosylation is inhibited by tunicamycin. These include a 90–100 kDa species still containing O ‐linked oligomannose chains, derived from a N ‐glycosylated material larger than 120 kDa; and a 30.5 kDa peptide lacking mannose residues, derived from a 33 kDa species. For both species, the growth temperature influences the level of incorporation of the non N ‐glycosylated molecules. Secretion of the peptides lacking N ‐linked saccharide chains follows the route defined by sec mutants.