Summary
Cells of Saccharomyces cerevisiae that have been growing exponentially for many generations contain low activities of lysosomal enzymes. In contrast to such fully adapted cells, differentiating or resting cells contain comparatively high activities of these enzymes. Thus, the digestive enzymes seem to be involved in the process of biochemical differentiation.
One of the four aminopeptidase isozymes present in extracts from yeast cells is localized in the vacuoles. This lysosomal enzyme can be separated from the other aminopeptidases by Sephadex G-150 gel filtration. Its specific activity is about 4 times higher in stationary cells than in exponentially growing cells.
Upon incubating protoplasts in a buffered sorbitol medium the activities of proteases and RNase increase significantly. A corresponding increase of lysosomal aminopeptidase activity occurs in the absence of glutamic acid or casein hydrolysate. Cycloheximide and actinomycin D inhibit the increase of lysosomal hydrolase activities in differentiating protoplasts. The observed changes of enzyme activities are probably due to induced synthesis of the respective proteins.
Similar content being viewed by others
References
Ambellan, E., Hollander, V. P.: A simplified assay for RNase activity in crude tissue extracts. Analyt. Biochem. 17, 474–484 (1966).
Beck, Ch., Meyenburg, H. K. v.: Enzyme pattern and aerobic growth of Saccharomyces cerevisiae under various degrees of glucose limitation. J. Bact. 96, 479–486 (1968).
Chapman, C., Bartley, W.: The kinetics of enzyme changes in yeast under conditions that cause the loss of mitochondria. Biochem. J. 107, 455–465 (1968).
Fukuhara, H.: Protein synthesis in non-growing yeast. Biochim. biophys. Acta (Amst.) 134, 143–164 (1967).
Gascón, S., Ottolenghi, P.: Invertase isozymes and their localization in yeast. C. R. Lab. Carlsberg 36, 85–93 (1967).
Halvorson, H. O.: Intracellular protein and nucleic acid turnover in resting yeast cells. Biochim. biophys. Acta (Amst.) 27, 255–266 (1958a).
— Studies on protein and nucleic acid turnover in growing cultures of yeast. Biochim. biophys. Acta (Amst.) 27, 267–276 (1958b).
Halvorson, H. O.: The induced synthesis of proteins. Advanc. Enzymol. 22, 99–156 (1960).
Hata, T., Hayashi, R., Doi, E.: Purification of yeast proteinases. I. Fractionation and some properties of the proteinases. Agr. biol. Chem. 31, 150–159 (1967).
Kroon, R. A. de, Koningsberger, V. V.: An inducible transport system for α-glucosides in protoplasts of Saccharomyces carlsbergensis. Biochim. biophys. Acta (Amst.) 204, 590–609 (1970).
Lampen, J. O.: External enzymes of yeast: their nature and formation. Antonie v. Leeuwenhoek 34, 1–18 (1968).
Matile, Ph.: Utilization of peptides in yeasts. In: Yeasts. Proc. 2nd Symp. on Yeasts, Bratislava 1966, p. 503–508. Bratislava: Publ. House of Slovak Acad. Sci. 1969.
Matile, Ph. Prospects of yeast cytology. Antonie v. Leeuwenhoek 35, Suppl.: Yeast Symposium 1969, 59–70 (1970).
— Wiemken, A.: The vacuole as the lysosome of the yeast cell. Arch. Mikrobiol. 56, 148–155 (1967).
Meyenburg, H. K. v.: Katabolit-Repression und der Sprossungszyklus von Saccharomyces cerevisiae. Vierteljahrschr. Naturforsch. Ges. Zürich 114, 113–222 (1969).
Scandalios, J. G.: Genetic control of multiples molecular forms of enzymes in plants: a review. Biochem. Gen. 3, 37–79 (1969).
Sylvén, B., Tobias, C. A., Malmgren, H., Ottoson, R., Thorell, B.: Cyclic variations in the peptidase and catheptic activities of yeast cultures synchronized with respect to cell multiplication. Exp. Cell Res. 16, 75–87 (1959).
Wiemken, A.: Eigenschaften der Hefevacuole. Doct. dissert., Swiss Fed. Inst. of Technol., Zürich 1969
— Matile, Ph., Moor, H.: Vacuolar dynamics in synchronously budding yeast Arch. Mikrobiol. 70, 89–103 (1970).
Author information
Authors and Affiliations
Additional information
The present work has been supported by the Swiss National Science Foundation.
Rights and permissions
About this article
Cite this article
Matile, P., Wiemken, A. & Guyer, W. A lysosomal aminopeptidase isozyme in differentiating yeast cells and protoplasts. Planta 96, 43–53 (1971). https://doi.org/10.1007/BF00397903
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00397903