Subcellular localization and glycoprotein nature of the invertase from the fission yeast Schizosaccharomyces pombe.
The subcellular localization of the enzyme invertase in Schizosaccharomyces pombe cells, both repressed and derepressed for synthesis of the enzyme, was studied. Most of the invertase was found to be located outside the plasma membrane and only a small percentage was found to be associated to membranes. A substantial portion of the external enzyme remained firmly bound to cell-wall material. All of the invertase recovered in soluble form from cellular extracts reacted with concanavalin A and with the lectin from Bandeiraea simplicifolia seeds, indicating the presence in the enzyme of a carbohydrate moiety which probably contains terminal mannosyl (or structurally related) and galactosyl residues. The possibility of the presence of two different forms of invertase in S. pombe was considered. An intracellular, soluble form of invertase, devoid of carbohydrate, similar to the small invertase of the budding yeast Saccharomyces cerevisiae, was not found in S. pombe. However, the Michaelis constant for sucrose of the enzyme present in repressed cells was smaller than that of the invertase synthesized under derepressing conditions, although this difference could also be the result of a different pattern of glycosylation of the invertase synthesized under different growth conditions.
D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000302:isolation & purification*; D006026:Glycoside Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D004718:Saccharomycetales / Q000201:enzymology*; D012568:Schizosaccharomyces / Q000201:enzymology*; D013347:Subcellular Fractions / Q000201:enzymology; D043324:beta-Fructofuranosidase
D006023:Glycoproteins; D006026:Glycoside Hydrolases; D043324:beta-Fructofuranosidase