Mutations affecting the signal sequence alter synthesis and secretion of yeast invertase.
Insertion mutations previously constructed within the proximal region of the yeast invertase signal sequence did not interfere with secretion or glycosylation of the enzyme. We now describe deletion mutations within the same signal sequence. Large deletions truncating the hydrophobic core of the signal peptide prevented both secretion and glycosylation of the enzyme and increased the intracellular concentration of nonglycosylated invertase. This increase was coupled with the appearance of a new invertase polypeptide, 2 kilodaltons larger than cytoplasmic invertase. The new polypeptide was consistent in size with uncleaved (signal peptide intact) pre-secretory invertase previously identified by using in vitro translation (apparent molecular mass, 62 kilodaltons). The data on enzyme activity indicate that invertase whose secretion is aborted by large deletion mutations augments the normal pool of cytoplasmic invertase found in sucrose-fermenting yeast cells.
D001483:Base Sequence; D005656:Fungal Proteins / Q000096:biosynthesis / Q000235:genetics* / Q000378:metabolism; D005786:Gene Expression Regulation; D006023:Glycoproteins / Q000096:biosynthesis; D006026:Glycoside Hydrolases / Q000096:biosynthesis / Q000235:genetics* / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D021382:Protein Sorting Signals / Q000235:genetics* / Q000502:physiology; D011994:Recombinant Proteins; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics*; D043324:beta-Fructofuranosidase
D005656:Fungal Proteins; D006023:Glycoproteins; D021382:Protein Sorting Signals; D011994:Recombinant Proteins; D006026:Glycoside Hydrolases; D043324:beta-Fructofuranosidase