6533b861fe1ef96bd12c4455
RESEARCH PRODUCT
Role of glycosylation in the incorporation of intrinsic mannoproteins into cell walls of Saccharomyces cerevisiae.
Pascual SanzEnrique HerreroRafael Sentandreusubject
chemistry.chemical_classificationGlycosylationGlycosylationMembrane GlycoproteinsTunicamycinSaccharomyces cerevisiaeMannosePeptideTunicamycinSaccharomyces cerevisiaeBiologybiology.organism_classificationMicrobiologyYeastcarbohydrates (lipids)Cell wallchemistry.chemical_compoundchemistryBiochemistryCell WallGeneticsGlycoproteinMolecular Biologydescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1989-02-01 | FEMS microbiology letters |