Proteinase activities of Saccharomyces cerevisiae during sporulation.
Sporulation in Saccharomyces cerevisiae occurs in the absence of a exogenous nitrogen source. Thus, the internal amino acid pool and the supply of nitrogen compounds from protein and nucleic acid turnover must be sufficient for new protein synthesis. Since sporulation involves an increased rate of protein turnover, an investigation was conducted of the changes in the specific activity of various proteinases. A minimum of 30% of the vegetative proteins was turned over during the course of sporulation. There was a 10- to 25-fold increase in specific activity of various proteinases, with a maximum activity around 20 h after transfer into the sporulation medium. The increase in activities was due to de novo synthesis since inhibition of protein synthesis by cycloheximide blocks both an increase in proteinase activities and sporulation. There was no increase observed in proteinase activities of nonsporogenic cultures (a and alpha/alpha strains) inoculated into the sporulation medium, suggesting that the increase in proteinase activities is "sporulation specific" and not a consequence of step-down conditions. The elution patterns through diethylaminoethyl-Sephadex chromatography of various proteinases extracted from T0 and T18 cells were similar, and no new species was observed.
D002474:Cell-Free System; D003513:Cycloheximide / Q000494:pharmacology; D005656:Fungal Proteins / Q000096:biosynthesis; D007700:Kinetics; D010447:Peptide Hydrolases / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000254:growth & development / Q000378:metabolism; D013172:Spores, Fungal / Q000201:enzymology / Q000254:growth & development / Q000378:metabolism
D005656:Fungal Proteins; D003513:Cycloheximide; D010447:Peptide Hydrolases