Abstract
Mannoproteins from cell walls of Saccharomyces cerevisiae synthesized at successive stages of the population growth cycle have been solubilized with Zymolyase and subsequently analyzed. The major change along the population cycle concerned a large size mannoprotein material; the size of the newly-synthesized molecules varied from 120,000-500,000 (mean of about 200,000) at early exponential phase to 250,000-350,000 (mean of about 300,000) at late exponential phase. These differences are due to modifications in the amount of N-glycosidically linked mannose residues, since the size of the peptide moiety was 90,000-100,000 at all growth stages and the level of O-glycosylation changed only slightly. After incubation of the purified walls with concanavalin A-ferritin and subsequent analysis by electron microscopy, labelling was localized at the external and internal faces of the walls. The middle space of these was labelled after digestion of the glucan network with Zymolyase, which demonstrate the presence of mannoproteins in close contact with the structural glucan molecules throughout the wall.
MeSH Terms
Cell Wall/analysis,ultrastructure
Chromatography, Gel
Concanavalin A
Dithiothreitol
Electrophoresis, Polyacrylamide Gel
Ferritins
Fungal Proteins/analysis,biosynthesis
Glucan Endo-1,3-beta-D-Glucosidase/metabolism
Glycoproteins/analysis,biosynthesis
Glycosylation
Membrane Glycoproteins
Microscopy, Electron
Molecular Weight
Saccharomyces cerevisiae/analysis,growth & development,metabolism,ultrastructure
Sodium Dodecyl Sulfate
Chemicals
Fungal Proteins
Glycoproteins
Membrane Glycoproteins
mannoproteins
Concanavalin A
Sodium Dodecyl Sulfate
Ferritins
Glucan Endo-1,3-beta-D-Glucosidase
Dithiothreitol
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Valentín E
Department de Microbiologia, Facultat de Farmacia, Universitat de València, Spain.
Herrero E
Rico H
Miragall F
Sentandreu R
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