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Yeast Genetics pp 167–203Cite as

Genetic Approaches to the Study of Protease Function and Proteolysis in Saccharomyces cerevisiae

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Part of the book series: Springer Series in Molecular Biology ((SSMOL))

Abstract

In the yeast Saccharomyces cerevisiae, proteases have been implicated in septum formation (Ulane and Cabib 1976), sporulation (Chen and Miller 1968; Hopper et al. 1974; Klar and Halvorson 1975; Betz and Weiser 1976; Zubenko and Jones 1981), protein turnover (Lopez and Gancedo 1979; Hansen et al. 1977), catabolite inactivation (Hägele et al. 1978; Neeff et al. 1978; Funayama et al. 1980; Holzer 1976; Jušik et al. 1976; Molano and Gancedo 1974; Magni et al. 1977; Magni et al. 1978), carbon starvation-induced degradation of NADP-dependent glutamate dehydrogenase (Hemmings and Mazon 1979; Mazon and Hemmings 1979), nitrogen starvation-induced degradation of NAD-dependent glutamate dehydrogenase (Hemmings 1980), enzyme secretion (Perlman and Halvorson 1981), localization of mitochondrial enzymes (Neupert and Schatz 1981), processing of enzyme precursors (Hemmings et al. 1981; Hasilik and Tanner 1978a, Jones et al. 1981; Zubenko et al. 1981), production of the pheromone α factor (J. Kurjan and I. Herskowitz 1982; D. Julius, A. Brake, L. Blair, and J. Thorner, personal communication), destruction of α factor (Maness and Edelman 1978; Ciejek and Thorner 1979; Ciejek 1980) and degradation of missense proteins (Donahue and Henry 1981) and nonsense fragments (Bigelis and Burridge 1978; Bigelis and Fink 1981).

Work in the author’s laboratory is supported by grants from the National Institutes of Health of the U.S. Public Health Service.

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References

  • Achstetter, T., Ehmann, C., Wolf, D. (1981). New proteolytic enzymes in yeast. Arch. Biochem. Biophys. 207:445–454.

    Article  PubMed  CAS  Google Scholar 

  • Aibara, S., Hayashi, R., Hata, T. (1971). Physical and chemical properties of yeast proteinase C. Agric. Biol. Chem. 35:658–666.

    Article  Google Scholar 

  • Bacon, J., Davidson, E., Jones, D., Taylor, I. (1966). The location of chitin in the yeast cell wall. Biochem. J. 101:36C–38C.

    PubMed  CAS  Google Scholar 

  • Bacon, J., Farmer, V., Jones, D., Taylor, I. (1969). The glucan components of the cell wall of bakers yeast (Saccharomyces cerevisiae) considered in relation to its ultrastructure. Biochem. J. 114:557–565.

    PubMed  CAS  Google Scholar 

  • Bakalkin, G., Kalnov, S., Zubatov, A., Luzikov, V. (1976). Degradation of total cell protein at different stages of Saccharomyces cerevisiae yeast growth. FEBS Lett. 63:218–221.

    Article  PubMed  CAS  Google Scholar 

  • Barth, R., Wolf, D., Holzer, H. (1978). Studies on the carboxypeptidase Y-inhibitor complex of yeast. Biochim. Biophys. Acta 527:63–69.

    PubMed  CAS  Google Scholar 

  • Bauer, H., Sigarlakie, E. (1975). Localization of alkaline phosphatase in Saccharomyces cerevisiae by means of ultrathin frozen sections. J. Ultrasr. Res. 50:208–215.

    Article  CAS  Google Scholar 

  • Beck, I., Fink, G. Wolf, D. (1980). The intracellular proteinases and their inhibitors in yeast. A mutant with altered regulation of proteinase A inhibitor activity. J. Biol. Chem. 255: 4821–4828.

    PubMed  CAS  Google Scholar 

  • Becker, J., Naider, F. (1980). Transport and utilization of peptides in yeast. In: Microorganisms and Nitrogen Sources, edited by J. Payne. New York: Wiley, pp. 257–275.

    Google Scholar 

  • Betz, H. (1975). Levels and turnover of the proteinase B inhibitors in yeast. Biochim. Biophys. Acta 404:142–151.

    PubMed  CAS  Google Scholar 

  • Betz, H. (1976). Inhibition of protein synthesis stimulates intracellular protein degradation in growing yeast cells. Biochem. Biophys. Res. Commun. 72:121–130.

    Article  PubMed  CAS  Google Scholar 

  • Betz, H. (1979). Loss of sporulation ability in a yeast mutant with low proteinase A levels. FEBS Lett. 100:171–174.

    Article  PubMed  CAS  Google Scholar 

  • Betz, H., Weiser, U. (1976). Protein degradation and proteinases during yeast sporulation. Eur. J. Biochem. 62:65–76.

    CAS  Google Scholar 

  • Betz, H., Hinze, H., Holzer, H. (1974). Isolation and properties of two inhibitors of proteinase B from yeast. J. Biol. Chem. 249:4515–4521.

    PubMed  CAS  Google Scholar 

  • Bigelis, R., Burridge, K. (1978). The immunological detection of yeast nonsense termination fragments on sodium dodecylsulfate—Polyacrylamide gels. Biochem. Biophys. Res. Commun. 82:322–327.

    Article  CAS  Google Scholar 

  • Bigelis, R., Fink, G. (1981). The HIS4 multifunctional protein: Immunochemistry of the wild type protein and altered forms. J. Biol. Chem. 256:5144–5152.

    PubMed  CAS  Google Scholar 

  • Böhni, P., Gasser, S., Leaver, C., Schatz, G. (1980). In: Structure and Expression of the Mitochondrial Genome, edited by A. M. Kroon and C. Sacconi. Amsterdam: North-Holland, pp. 423–433.

    Google Scholar 

  • Bucking-Throm, E., Düntze, W., Hartwell, L., and Manney, T. (1973). Reversible arrest of haploid yeast cells at the initiation of DNA synthesis by a diffusible sex factor. Exp. Cell Res. 76:99–110.

    Article  PubMed  CAS  Google Scholar 

  • Bünning, P., Holzer, H. (1977). Natural occurrence and chemical modification of proteinase B inhibitors from yeast. J. Biol. Chem. 252:5316–5323.

    PubMed  Google Scholar 

  • Cabib, E., Bowers, B. (1971). Chitin and yeast budding. Localization of chitin in yeast bud scars. J. Biol. Chem. 246:152–159.

    PubMed  CAS  Google Scholar 

  • Chan, R., Otte, C. (1982a). Isolation and genetic analysis of Saccharomyces cerevisiae mutants supersensitive to G1 arrest by a-factor and α-factor pheromone. Mol. Cell. Biol. 2:11–20.

    PubMed  CAS  Google Scholar 

  • Chan, R., Otte, C. (1982b). Physiological characterization of Saccharomyces cerevisiae mutants supersensitive to G1 arrest by a-factor and α-factor pheromone. Mol. Cell. Biol. 2:21–29.

    PubMed  CAS  Google Scholar 

  • Chen, A., Miller, J. (1968). Proteolytic activity of intact yeast cells during sporulation. Can. J. Microbiol. 14:957–963.

    Article  PubMed  CAS  Google Scholar 

  • Ciejek, E. (1980). Alpha-factor, an oligopeptide pheromone from Saccharomyces cerevisiae: Purification, chemical synthesis and cell-mediated proteolysis. Ph.D. Thesis, University of California, Berkeley.

    Google Scholar 

  • Ciejek, E., Thorner, J. (1979). Recovery of S. cerevisiae a cells from G1 arrest by α-factor pheromone requires endopeptidase action. Cell 18:623–635.

    Article  PubMed  CAS  Google Scholar 

  • Dietlein, G., Schweizer, E. (1975). Control of fatty acid biosynthesis in Saccharomyces cerevisiae. Eur. J. Biochem. 58:177–184.

    Article  PubMed  CAS  Google Scholar 

  • Doi, E., Hayashi, R., Hata, T. (1967). Purification of yeast proteinases II. Purification and some properties of yeast proteinase C. Agric. Biol. Chem. 31:160–169.

    Article  CAS  Google Scholar 

  • Donahue, T., Henry, S. (1981). Myoinositol-1-phosphate synthase: characteristics of the enzyme and identification of its structural gene in yeast. J. Biol. Chem. 256:7077–7085.

    PubMed  CAS  Google Scholar 

  • Diintze, W., MacKay, V., Manney, T. (1970). Saccharomyces cerevisiae: A diffusible sex factor. Science 168:1472–1473.

    Article  Google Scholar 

  • Diintze, W., Stötzler, D., Bucking-Throm, E., Kalbitzer, S. (1973). Purification and partial characterization of α-factor, a mating-type specific inhibitor of cell reproduction from S. cerevisiae. Eur. J. Biochem. 35:357–365.

    Article  Google Scholar 

  • Duran, A., Bowers, B., Cabib, E. (1975). Chitin synthetase zymogen is attached to the yeast plasma membrane. Proc. Natl. Acad. Sci. USA 72:3952–3955.

    Article  PubMed  CAS  Google Scholar 

  • Esmon, B., Novick, P., Schekman, R. (1981). Compartmentalized assembly of oligosaccharides on exported glycoproteins in yeast. Cell 25:451–460.

    Article  PubMed  CAS  Google Scholar 

  • Félix, F., Brouillet, N. (1966). Purification and propriétés de deux peptidases de levure de brasserie. Biochim. Biophys. Acta 122:127–144.

    PubMed  Google Scholar 

  • Ferguson, Jr., J., Boll, M., Holzer, H. (1967). Yeast malate dehydrogenase: enzyme inactivation in catabolite repression. Eur. J. Biochem 1:21–25.

    Article  PubMed  CAS  Google Scholar 

  • Fink, G., Styles, C. (1974). Gene conversion of deletions in the HIS4 region of yeast. Genetics 77:231–244.

    PubMed  CAS  Google Scholar 

  • Finkelstein, D., Strausberg, S. (1979). Metabolism of α-factor by a mating type cells of Saccharomyces cerevisiae. J. Biol. Chem. 254:796–803.

    PubMed  CAS  Google Scholar 

  • Fischer, E., Holzer, H. (1980). Interaction of proteinases and their inhibitors from yeast. Biochim. Biophys. Acta 615:187–198.

    PubMed  CAS  Google Scholar 

  • Frey, J., Röhm, K. -H. (1978). Subcellular localization and levels of aminopeptidases and dipeptidase in Saccharomyces cerevisiae. Biochim. Biophys. Acta 527:31–41.

    PubMed  CAS  Google Scholar 

  • Frey, J., Röhm, K. -H. (1979a). External and internal forms of yeast aminopeptidase II. Eur. J. Biochem. 97:169–173.

    Article  PubMed  CAS  Google Scholar 

  • Frey, J., Röhm, K. -H. (1979b). The glucose-induced inactivation of aminopeptidase I in Saccharomyces cerevisiae. FEBS Lett. 100:261–264.

    Article  PubMed  CAS  Google Scholar 

  • Fujishiro, K., Sanada, Y., Tanaka, H., Katunuma, N. (1980). Purification and characterization of yeast proteinase B. J. Biochem. 87:1321–1326.

    PubMed  CAS  Google Scholar 

  • Funayama, S., Gancedo, J., Gancedo, C. (1980). Turnover of yeast fructosebisphos-phatase in different metabolic condition. Eur. J. Biochem. 109:61–66.

    Article  PubMed  CAS  Google Scholar 

  • Gancedo, C. (1971). Inactivation of fructose 1,6-diphosphatase by glucose in yeast. J. Bacteriol. 107:401–405.

    PubMed  CAS  Google Scholar 

  • Gancedo, C., Schwerzmann, J. (1976). Inactivation by glucose of phosphoenolpyruvate carboxykinase from Saccharomyces cerevisiae. Arch. Microbiol. 109:221–225.

    CAS  Google Scholar 

  • Gorts, C. (1969). Effect of glucose on the activity and the kinetics of the maltose uptake system and of α-glucosidase in Saccharomyces cerevisiae. Biochim. Biophys. Acta 184:299–305.

    PubMed  CAS  Google Scholar 

  • Hägele, E., Neeff, J. Mecke, D. (1978). The malate dehydrogenase isoenzymes of Saccharomyces cerevisiae. Eur. J. Biochem. 83:67–76.

    Article  PubMed  Google Scholar 

  • Halvorson, H. (1958a). Intracellular protein and nucleic acid turnover in resting yeast cells. Biochim. Biophys. Acta 27:255–266.

    Article  PubMed  CAS  Google Scholar 

  • Halvorson, H. (1958b). Studies on protein and nucleic acid turnover in growing cultures of yeast. Biochim. Biophys. Acta 27:267–276.

    Article  PubMed  CAS  Google Scholar 

  • Hansen, R., Switzer, R., Hinze, H., Holzer, H. (1977). Effects of glucose and nitrogen source on the levels of proteinases, peptidases, and proteinase inhibitors in yeast. Biochim. Biophys. Acta 196:103–114.

    Google Scholar 

  • Hartwell, L., Culotti, J., Reid, B. (1970). Genetic control of the cell-division cycle in yeast. I. Detection of mutants. Proc. Natl. Acad. Sci. USA 66:352–359.

    Article  CAS  Google Scholar 

  • Hashimoto, C., Cohen, R., Zhang, W. -J. Ballou, C. (1981). Carbohydrate chains on yeast carboxypeptidase Y are phosphorylated. Proc. Natl. Acad. Sci. USA 78:2244–2248.

    Article  PubMed  CAS  Google Scholar 

  • Hasilik, A. (1974). Inactivation of chitin synthase in Saccharomyces cerevisiae. Arch. Microbiol. 101:295–301.

    Article  PubMed  CAS  Google Scholar 

  • Hasilik, A. (1980): Biosynthesis of lysosomal enzymes. Trends Biochem. Sci. 4:237–240.

    Article  Google Scholar 

  • Hasilik, A., Neufeld, E. (1980). Biosynthesis of lysosomal enzymes in fibroblasts. J. Biol. Chem. 255:4946–4950.

    PubMed  CAS  Google Scholar 

  • Hasilik, A., Tanner, W. (1976a). Biosynthesis of carboxypeptidase Y in yeast. Evidence for a precursor form of the glycoprotein. Biochem. Biophys. Res. Commun. 72:1430–1436.

    CAS  Google Scholar 

  • Hasilik, A., Tanner, W. (1978a). Biosynthesis of the vacuolar yeast glycoprotein carboxypeptidase Y. Conversion of precursor into enzyme. Eur. J. Biochem. 91:567–575.

    Article  PubMed  CAS  Google Scholar 

  • Hasilik, A., Tanner, W. (1978b). Carbohydrate moiety of carboxypeptidase Y and perturbation of its biosynthesis. Eur. J. Biochem. 91:567–575.

    Article  PubMed  CAS  Google Scholar 

  • Hasilik, A., Müller, H., Holzer, H. (1974). Compartmentation of the tryptophan-synthetase proteolyzing system in Saccharomyces cerevisiae. Eur. J. Biochem. 48:111–117.

    Article  CAS  Google Scholar 

  • Hayashi, R., Aibara, S., Hata, T. (1970). A unique carboxypeptidase activity of yeast proteinase C. Biochim. Biophys. Acta 212:359–361.

    PubMed  CAS  Google Scholar 

  • Hata, T., Hayashi, R., Doi, E. (1967a). Purification of yeast proteinases I. Fractionation and some properties of these proteinases. Agric. Biol. Chem. 31:150–159.

    Article  CAS  Google Scholar 

  • Hata, T., Hayashi, R., Doi, E. (1967b). Purification of yeast proteinases. III. Isolation and physicochemical properties of yeast proteinase A and C. Agric. Biol. Chem. 31:357–367.

    Article  CAS  Google Scholar 

  • Hayashi, R., Moore, S., and Stein, W. (1973). Carboxypeptidase from yeast. Large scale preparation and the application to COOH-terminal analysis of peptides and proteins. J. Biol. Chem. 248:2296–2302.

    PubMed  CAS  Google Scholar 

  • Hemmings, B. (1980). Phosphorylation and proteolysis regulate the NAD-dependent glutamate dehydrogenase from Saccharomyces cerevisiae. FEBS Lett. 122:297–302.

    Article  PubMed  CAS  Google Scholar 

  • Hemmings, B., Mazon, M. (1979). Proteolytic degradation of NADP-dependent glutamate dehydrogenase in yeast. In: Limited Proteolysis in Microorganisms, edited by H. Holzer and G. Cohen. DHEW Publ. No. 79–1591, pp. 69–75.

    Google Scholar 

  • Hemmings, G., Zubenko, G., Jones, E. (1980). Proteolytic inactivation of the NADP-dependent glutamate dehydrogenase in proteinase-deficient mutants of Saccharomyces cerevisiae. Arch. Biochem. Biophys. 202:657–660.

    Article  PubMed  CAS  Google Scholar 

  • Hemmings, B., Zubenko, G., Hasilik, A., Jones, E. (1981). Mutant defective in processing of an enzyme located in the lysosome-like vacuole of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 78:435–439.

    Article  PubMed  CAS  Google Scholar 

  • Hinze, H., Betz, H., Saheki, T., Holzer, H. (1975). Formation of a complex between yeast proteinases A and B. Hoppe-Seyler’s Z. Physiol. Chem. 356:1259–1264.

    CAS  Google Scholar 

  • Holzer, H. (1976). Catabolite inactivation in yeast. Trends Biochem. Sci. 1:178–181.

    CAS  Google Scholar 

  • Hopper, A., Magee, P., Welch, S., Friedman, M., Hall, B. (1974). Macromolecule synthesis and breakdown in relation to sporulation and meiosis in yeast. J. Bacteriol. 119:619–628.

    PubMed  CAS  Google Scholar 

  • Johnson, M. (1941). Isolation and properties of a pure yeast polypeptidase. J. Biol. Chem. 137:575–586.

    CAS  Google Scholar 

  • Jones, E. (1977). Proteinase mutants of Saccharomyces cerevisiae. Genetics 85:23–33.

    PubMed  CAS  Google Scholar 

  • Jones, E., Zubenko, G., Parker, R., Hemmings, B., Hasilik, A. (1981). Pleiotropic mutations of S. cerevisiae which cause deficiency for proteinases and other vacuole enzymes. Alfred Benzon Symposium 16:182–198, edited by D. von Wettstein, J. Friis, M. Kielland-Brandt, A. Stenderup. Copenhagen: Munksgaard.

    Google Scholar 

  • Jones, E., Zubenko, G., Parker, R. (1982). PEP4 gene function is required for expression of several vacuolar hydrolases in Saccharomyces cerevisiae. Genetics 102:665–677.

    PubMed  CAS  Google Scholar 

  • Jušik, M., Hinze, H., Holzer, H. (1976). Inactivation of yeast enzymes by proteinase A and B and carboxypeptidase Y from yeast. Hoppe-Seyler’s Z. Physiol. Chem. 357:735–740.

    Article  Google Scholar 

  • Kaneko, Y., Toh-e, A., Oshima, Y. (1982). Identification of the structural gene and a new regulatory gene for the synthesis of repressible alkaline phosphatase in Saccharomyces cerevisiae. Mol. Cell. Biol. 2:127–137.

    PubMed  CAS  Google Scholar 

  • Keesey, Jr., J., Bigelis, R., Fink, G. (1979). The product of the HIS4 gene cluster in Saccharomyces cerevisiae: a trifunctional polypeptide. J. Biol. Chem. 254:7427–7433.

    PubMed  CAS  Google Scholar 

  • Kenny, A., Booth, A., George, S., Ingram, J., Kershaw, D., Wood, E., and Young, A. (1976). Dipeptidyl peptidase IV, a kidney brush-border serine peptidase. Biochem. J. 157:169–182.

    PubMed  CAS  Google Scholar 

  • Klar, A., Halvorson, H. (1975). Proteinase activities of Saccharomyces cerevisiae. J. Bacteriol. 124:863–869.

    PubMed  CAS  Google Scholar 

  • Kominami, E., Hoffschulte, H., Holzer, H. (1981a). Purification and properties of proteinase B from yeast. Biochim. Biophys. Acta 661:124–135.

    CAS  Google Scholar 

  • Kominami, E., Hoffschulte, H. Leuschel, L., Maier, K., Holzer, H. (1981b). The substrate specificity of proteinase B from baker’s yeast. Biochim. Biophys. Acta 661:136–141.

    PubMed  CAS  Google Scholar 

  • Kreil, G., Mollay, C., Kaschnitz, R., Haiml, L., Vilas, U. (1980a). Prepromellitin: specific cleavage of the pre and the propeptide in vitro. Ann. N.Y. Acad. Sci. 343:338–346.

    Article  PubMed  CAS  Google Scholar 

  • Kreil, G., Haiml, L., Suchanek, G. (1980b). Stepwise cleavage of the pro part of promellitin by dipeptidylpeptidase IV. Eur. J. Biochem. 111:49–58.

    Article  PubMed  CAS  Google Scholar 

  • Kuhn, R., Walsh, K., Neurath, H. (1974). Isolation and characterization of an acid carboxypeptidase from yeast. Biochemistry 13:3871–3877.

    Article  PubMed  CAS  Google Scholar 

  • Kuhn, R., Walsh, K., Neurath, H. (1976). Reaction of yeast carboxypeptidase C with group specific reagents. Biochemistry 15:4881–4885.

    Article  PubMed  CAS  Google Scholar 

  • Kurjan, J., Herskowitz, I. (1982). Structure of a yeast pheromone gene (MFα): a putative α-factor precursor contains four tandem copies of mature α-factor. Cell 30:933–943.

    Article  PubMed  CAS  Google Scholar 

  • Lenney, J. (1975). Three yeast proteins that specifically inhibit yeast proteases A, B and C. J. Bacteriol. 122:1265–1273.

    PubMed  CAS  Google Scholar 

  • Lenney, J., Dalbec, J. (1967). Purification and properties of two proteinases from Saccharomyces cerevisiae. Arch. Biochem. Biophys. 120:42–48.

    Article  PubMed  CAS  Google Scholar 

  • Lenney, J., Matile, P., Wiemken, A., Schellenberg, M., Meyer, J. (1974). Activities and cellular localization of yeast proteinases and their inhibitors. Biochem. Biophys. Res. Commun. 60:1378–1383.

    Article  CAS  Google Scholar 

  • Lewin, A., Gregor, I., Mason, T., Nelson, N., Schatz, G. (1980). Cytoplasmically made subunits of yeast mitochondrial Fr ATPase and cytochrome c oxidase are synthesized as individual precursors, not as polyproteins. Proc. Natl. Acad. Sci. USA 77:3998–4002.

    Article  PubMed  CAS  Google Scholar 

  • Löffier, H. -G., Röhm, K. -H. (1979). Comparative studies on the dodecameric and hexameric forms of yeast aminopeptidase I. Z. Naturforsch 34c:381–386.

    Google Scholar 

  • Looze, Y., Gillet, L., Deconinck, M., Couteaux, B., Polastro, E., Leonis, J. (1979). Protease B from Saccharomyces cerevisiae. Int. J. Peptide Protein Res. 13:253–259.

    Article  CAS  Google Scholar 

  • Lopez, S., Gancedo, J. (1979). Effect of metabolic condition on protein turnover in yeast. Biochem. J. 178:769–776.

    PubMed  CAS  Google Scholar 

  • Maccechini, M. -L., Rudin, Y., Blobel, G., Schatz, G. (1979a). Import of proteins into mitochondria: precursor forms of the extramitochondrially made F1-ATPase subunits in yeast. Proc. Natl. Acad. Sci. USA 76:343–347.

    Article  Google Scholar 

  • Maccechini, M. -L., Rudin, Y., Schatz, G. (1979b). Transport of proteins across mitochondrial outer membrane. A precursor form of the cytoplasmically made intermembrane enzyme cytochrome c peroxidase. J. Biol. Chem. 254:7468–7471.

    Google Scholar 

  • Magni, G., Santarelli, I., Natalini, P., Ruggieri, S., Vita, A. (1977). Catabolite inactivation of bakers yeast uridine nucleosidase. Isolation and partial purification of a specific proteolytic inactivase. Eur. J. Biochem. 75:77–82.

    Article  PubMed  CAS  Google Scholar 

  • Magni, G., Pallotta, G., Natalini, P., Ruggieri, S., Santarelli, I., Vita, A. (1978). Inactivation of uridine nucleosidase in yeast. Purification and properties of an inactivating protein. J. Biol. Chem. 253:2501–2503.

    PubMed  CAS  Google Scholar 

  • Magni, G., Natalini, P., Santarelli, I., Ruggieri, S., Vita, A. (1979). Inactivation of bakers yeast uridine nucleosidase. In: Limited Proteolysis in Microorganisms, edited by H. Holzer, G. Cohen. DHEW Publ. No. 79–1591, pp. 87–96.

    Google Scholar 

  • Maier, K., Müller, H., Holzer, H. (1979a). Purification and molecular characterization of two inhibitors of yeast proteinase B. J. Biol. Chem. 254:8491–8497.

    PubMed  CAS  Google Scholar 

  • Maier, K., Müller, H., Tesch, R., Trolp, R., Witt, I., Holzer, H. (1979b). Primary structure of yeast proteinase B inhibitor 2. J. Biol. Chem. 254:12555–12561.

    PubMed  CAS  Google Scholar 

  • Maier, K., Müller, H., Tesch, R., Witt, I., Holzer, H. (1979c). Amino acid sequence of yeast proteinase B inhibitor 1 comparison with inhibitor 2. Biochem. Biophys. Res. Commun. 91:1390–1398.

    Article  PubMed  CAS  Google Scholar 

  • Maness, P., Edelman, G. (1978). Inactivation and chemical alteration of mating factor α by cells and spheroplasts of yeast. Proc. Natl. Acad. Sci. USA 75: 1304–1308.

    Article  PubMed  CAS  Google Scholar 

  • Marriott, M., Tanner, W. (1979). Localization of dolichyl phosphate- and pyrophos-phate-dependent glycosyl transfer reactions in Saccharomyces cerevisiae. J. Bacteriol. 139:565–572.

    CAS  Google Scholar 

  • Masuda, T., Hayashi, R., Hata, T. (1975). Aminopeptidases in the acidic fraction of the yeast autolysate. Agric. Biol. Chem. 39:499–505.

    Article  CAS  Google Scholar 

  • Matern, H., Holzer, H. (1977). Catabolite inactivation of the galactose uptake system in yeast. J. Biol. Chem. 252:6399–6402.

    PubMed  CAS  Google Scholar 

  • Matern, H., Betz, H., Holzer, H. (1974a). Compartmentation of inhibitors of proteinases A and B and carboxypeptidase Y in yeast. Biochem. Biophys. Res. Commun. 60:1051–1057.

    CAS  Google Scholar 

  • Matern, H., Hoffman, M., Holzer, H. (1974b). Isolation and characterization of the carboxypeptidase Y inhibitors from yeast. Proc. Natl. Acad. Sci. USA 71:4874–4878.

    Article  PubMed  CAS  Google Scholar 

  • Matern, H., Barth, R., Holzer, H. (1979). Chemical and physical properties of the carboxypeptidase Y inhibitor from bakers yeast. Biochim. Biophys. Acta 567:503–510.

    PubMed  CAS  Google Scholar 

  • Matile, P., Wiemken, A. (1967). The vacuole as the lysosome of the yeast cell. Arch. Mikrobiol. 56:148–155.

    Article  PubMed  CAS  Google Scholar 

  • Matile, P., Wiemken, A., Guyer, W. (1971). A lysosomal aminopeptidase isozyme in differentiating yeast cells and protoplasts. Planta 96:43–53.

    Article  CAS  Google Scholar 

  • Mazon, M. (1978). Effect of glucose starvation on the nicotinamide adenine dinucleotide phosphate-dependent glutamate dehydrogenase of yeast. J. Bacteriol. 133:780–785.

    PubMed  CAS  Google Scholar 

  • Mazon, M., Hemmings, B. (1979). Regulation of Saccharomyces cerevisiae nicotinamide adenine dinucleotide phosphate-dependent glutamate dehydrogenase by proteolysis during carbon starvation. J. Bacteriol. 139:686–689.

    PubMed  CAS  Google Scholar 

  • McLellan, Jr., W., Lampen, J. (1963). The acid phosphatase of yeast: localization and secretion by protoplasts. Biochim. Biophys. Acta 67:324–326.

    Article  PubMed  CAS  Google Scholar 

  • Mechler, B., Wolf, D. (1981). Analysis of proteinase A function in yeast. Eur. J. Biochem. 121:47–52.

    Article  PubMed  CAS  Google Scholar 

  • Mechler, B., Müller, M., Müller, H., Muessdoerffer, F., Wolf, D. (1982). In vivo biosynthesis of the vacuolar proteinases A and B in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 257:11203–11206.

    PubMed  CAS  Google Scholar 

  • Metz, G., Röhm, K. -H. (1978). Yeast aminopeptidase I. Chemical composition and catalytic properties. Biochim. Biophys. Acta 429:933–949.

    Google Scholar 

  • Metz, R., Marx, E., Röhm, K. -H. (1977). The quaternary structure of yeast aminopeptidase I. Z. Naturforsch. 32c:929–937.

    CAS  Google Scholar 

  • Mihara, K., Blobel, G. (1980). The four cytoplasmically made subunits of yeast mitochondrial cytochrome c oxidase are synthesized individually and not as a polyprotein. Proc. Natl. Acad. Sci. USA 77:4160–4164.

    Article  PubMed  CAS  Google Scholar 

  • Molano, J., Gancedo, C. (1974). Specific inactivation of fructose 1,6-bisphosphatase from Saccharomyces cerevisiae by a yeast protease. Eur. J. Biochem. 44:213–217.

    Article  PubMed  CAS  Google Scholar 

  • Mortimer, R., Schild, D. (1982). Genetic map of Saccharomyces cerevisiae. In: The Molecular Biology of the Yeast Saccharomyces. Metabolism and Gene Expression, edited by J. Strathern, E. Jones, J. Broach. Cold Spring Harbor, N. Y.: Cold Spring Harbor Laboratory, pp. 639–650.

    Google Scholar 

  • Muessdoerffer, F. (1980). Occurrence of proteinase A isoinhibitors in wild type yeast strains and commercial bakers yeast. Biochem. Biophys. Res. Commun. 97:423–429.

    Article  Google Scholar 

  • Muessdoerffer, F., Tortora, P., Holzer, H. (1980). Purification and properties of proteinase A from yeast. J. Biol. Chem. 255:12087–12093.

    Google Scholar 

  • Neeff, J., Hagele, E., Nauhaus, J., Heer, U., Mecke, D. (1978). Evidence for catabolite degradation in the glucose-dependent inactivation of yeast cytoplasmic malate dehydrogenase. Eur. J. Biochem. 87:489–495.

    Article  PubMed  CAS  Google Scholar 

  • Nelson, N., Schatz, G. (1979). Energy-dependent processing of cytoplasmically made precursors to mitochondrial proteins: Proc. Natl. Acad. Sci. USA 76:4365–4369.

    Article  PubMed  CAS  Google Scholar 

  • Neupert, W., Schatz, G. (1981). How proteins are transported into mitochondria. Trends Biochem. Sci. 6:1–4.

    Article  CAS  Google Scholar 

  • Novick, P., Ferro, S., Schekman, R. (1981). Order of events in the yeast secretory pathway. Cell 25:461–469.

    Article  PubMed  CAS  Google Scholar 

  • Nunez de Castro, I., Holzer, H. (1976). Studies on the proteinase A inhibitor IA 3 from yeast. Hoppe-Seyler’s Z. Physiol. Chem. 357:727–734.

    Article  CAS  Google Scholar 

  • Perlman, D., Halvorson, H. (1981). Distinct repressible mRNAs for cytoplasmic and secreted yeast invertase are encoded by a single gene. Cell 25:525–536.

    Article  PubMed  CAS  Google Scholar 

  • Pilar-Fernandez, M., Correa, J., Cabib, E. (1982). Activation of chitin synthetase in permeabilized cells of a Saccharomyces cerevisiae mutant lacking proteinase B. J. Bacteriol. 152:1255–1264.

    Google Scholar 

  • Robertson, J., Halvorson, H. (1957). The components of maltozymase in yeast and their behavior during deadaptation. J. Bacteriol. 73:186–198.

    PubMed  CAS  Google Scholar 

  • Röhm, K. -H. (1974). Properties of a highly purified dipeptidase from brewers yeast. Hoppe-Seyler’s Z. Physiol. Chem. 355:675–686.

    Article  Google Scholar 

  • Rose, B., Becker, J. Naider, F. (1979). Peptidase activities in Saccharomyces cerevisiae. J. Bacteriol. 139:220–224.

    PubMed  CAS  Google Scholar 

  • Saheki, T., Matsuda, Y., Holzer, H. (1974). Purification and characterization of macromolecular inhibitors of proteinase A from yeast. Eur. J. Biochem. 47:325–332.

    Article  PubMed  CAS  Google Scholar 

  • Sanada, Y., Fujishiro, K., Tanaka, H., Katanuma, N. (1975). Isolation and characterization of yeast protease B. Biochem. Biophys. Res. Commun. 86:815–821.

    Article  Google Scholar 

  • Schweizer, E., Kuhn, L., Castorph, H. (1971). A new gene cluster in yeast: the fatty acid synthetase system. Hoppe-Seyler’s Z. Physiol. Chem. 352:3277–3284.

    Google Scholar 

  • Schweizer, E., Werkmeister, K., Jain, M. (1978). Fatty acid biosynthesis in yeast. Mol. Cell. Biochem. 21:95–106.

    CAS  Google Scholar 

  • Skudlarek, M., Swank, R. (1979). Biosynthesis of two lysosomal enzymes in macrophages. J. Biol. Chem. 254:9939–9942.

    PubMed  CAS  Google Scholar 

  • Sprague, Jr., G., Herskowitz, I. (1981). Control of yeast cell type by the mating type locus. I. Identification and control of expression of the a-specific gene, BARI. J. Mol. Biol. 153:305–321.

    Article  PubMed  CAS  Google Scholar 

  • Sprague, Jr., G., Rine, J., Herskowitz, I. (1981). Control of yeast cell type by the mating type locus. II. Genetic interactions between MATa and unlinked a-specific STE genes. J. Mol. Biol. 153:323–335.

    Article  PubMed  CAS  Google Scholar 

  • Steiner, D., Quinn, P., Chan, S., Marsh, J., Tager, H. (1980). Processing mechanisms in the biosynthesis of proteins. Ann. N.Y. Acad. Sci. 343:1–16.

    Article  PubMed  CAS  Google Scholar 

  • Stern, A., Jones, B., Shively, J., Stein, S., Udenfriend, S. (1981). Two adrenal opiod polypeptides: proposed intermediates in the processing of proenkephalin. Proc. Natl. Acad. Sci. USA 78:1962–1966.

    Article  PubMed  CAS  Google Scholar 

  • Stevens, T. Esmon, B., Schekman, R. (1982). Early stages in the yeast secretory path-way are required for transport of carboxypeptidase Y to the vacuole. Cell 30:439–448.

    Article  PubMed  CAS  Google Scholar 

  • Stewart, J., Sherman, F., Shipman, N., Jackson, M. (1971). Identification and mutational relocation of the AUG codon initiating transcription of iso-1-cytochrome c in yeast. J. Biol. Chem. 246:7429–7445.

    PubMed  CAS  Google Scholar 

  • Stötzler, D., Düntze, W. (1976). Isolation and characterization of four related peptides exhibiting α-factor activity from Saccharomyces cerevisiae. Eur. J. Biochem. 65:257–262.

    Article  PubMed  Google Scholar 

  • Suarez-Rendueles, M., Schwencke, J., Garcia-Alvarez, N., Gascon, S. (1981). A new X-prolyl-dipeptidyl aminopeptidase from yeast associated with a particulate fraction. FEBS Lett. 131:296–300.

    Article  CAS  Google Scholar 

  • Sumrada, R., Cooper, T. (1978). Control of vacuole permeability and protein degradation by the cell cycle arrest signals in Saccharomyces cerevisiae. J. Bacteriol. 136:234–246.

    PubMed  CAS  Google Scholar 

  • Sutton, D., Lampen, J. (1962). Localization of sucrose and maltose fermenting systems in Saccharomyces cerevisiae. Biochim. Biophys. Acta 56:303–312.

    CAS  Google Scholar 

  • Trimble, R., Maley, F. (1977). The use of endo-β-N-acetylglucosaminidase H in characterizing the structure and function of glycoproteins. Biochem. Biophys. Res. Commun. 78:935–944.

    CAS  Google Scholar 

  • Trumbly, R. (1980). A genetic and biochemical study of the aminopeptidases of Saccharomyces cerevisiae. Ph.D. Thesis. University of California, Davis.

    Google Scholar 

  • Ulane, R., Cabib, E. (1974). The activating system of chitin synthetase from Saccharomyces cerevisiae. Purification and properties of an inhibitor of the activating factor. J. Biol. Chem. 249:3418–3422.

    PubMed  CAS  Google Scholar 

  • Ulane, R., Cabib, E. (1976). The activating system of chitin synthetase from Saccharomyces cerevisiae. J. Biol. Chem. 251:3367–3374.

    PubMed  CAS  Google Scholar 

  • Whitney, P., Cooper, T., Magasanik, B. (1973). The induction of urea carboxylase and allophanate hydrolase in Saccharomyces cerevisiae. J. Biol. Chem. 248:6203–6209.

    PubMed  CAS  Google Scholar 

  • Wiemken, A., Schellenberg, M., Urech, K. (1979). Vacuoles: the sole compartment of digestive enzymes in yeast (Saccharomyces cerevisiae)? Arch. Microbiol. 123:23–35.

    CAS  Google Scholar 

  • Witt, L, Kronau, R., Holzer, H. (1966). Isoenzyme der malat-dehydrogenase und ihre regulation in Saccharomyces cerevisiae. Biochim. Biophys. Acta 128:63–73.

    PubMed  CAS  Google Scholar 

  • Wolf, D., Ehmann, C. (1978a). Isolation of yeast mutants lacking proteinase B activity. FEBS Lett. 92:121–124.

    Article  CAS  Google Scholar 

  • Wolf, D., Ehmann, C. (1978b). Carboxypeptide S from yeast: regulation of its activity during vegetative growth and sporulation. FEBS Lett. 91:59–62.

    Article  PubMed  CAS  Google Scholar 

  • Wolf, D., Ehmann, C. (1979). Studies on a proteinase B mutant of yeast. Eur. J. Biochem. 98:375–384.

    Article  PubMed  CAS  Google Scholar 

  • Wolf, D., Ehmann, C. (1981). Carboxypeptidase S- and carboxypeptidase Y-deficient mutants of Saccharomyces cerevisiae. J. Bacteriol. 147:418–426.

    PubMed  CAS  Google Scholar 

  • Wolf, D., Fink, G. (1975). Proteinase C (carboxypeptidase Y) mutant of yeast. J. Bacteriol. 123:1150–1156.

    PubMed  CAS  Google Scholar 

  • Wolf, D., Weiser, U. (1977). Studies on a carboxypeptidase Y mutant of yeast and evidence for a second carboxyptidase activity. Eur. J. Biochem. 73:553–556.

    Article  PubMed  CAS  Google Scholar 

  • Wolf, D., Ehmann, C., Beck, I. (1979). Genetic and biochemical analysis of intracellular proteolysis in yeast. In: Biological Functions of Proteinases, edited by H. Holzer and H. Tschesche. New York: Springer-Verlag, pp. 55–72.

    Google Scholar 

  • Zubenko, G. (1981). A genetic approach to the study of intracellular proteolysis in Saccharomyces cerevisiae. Ph.D. Thesis. Carnegie-Mellon University, Pittsburgh, Pennsylvania.

    Google Scholar 

  • Zubenko, G., Jones, E. (1979). Catabolite inactivation of gluconeogenic enzymes in mutants of yeast deficient in proteinase B. Proc. Natl. Acad. Sci. USA 76:4581–4585.

    Article  PubMed  CAS  Google Scholar 

  • Zubenko, G., Jones, E. (1981). Protein degradation, meiosis and sporulation in proteinase-deficient mutants of Saccharomyces cerevisiae. Genetics 97:45–64.

    PubMed  CAS  Google Scholar 

  • Zubenko, G., Mitchell, A., Jones, E. (1979). Septum formation, cell division and sporulation in mutants of yeast deficient in proteinase B. Proc. Natl. Acad. Sci. 76:2395–2399.

    Article  PubMed  CAS  Google Scholar 

  • Zubenko, G., Mitchell, A., Jones, E. (1980). Mapping of the proteinase B structural gene, PRB1, in Saccharomyces cerevisiae and identification of nonsense alleles within the locus. Genetics 96:137–146.

    PubMed  CAS  Google Scholar 

  • Zubenko, G., Park, F., Jones, E. (1981). PEP4 gene function is required for maturation of vacuolar hydrolases. In: Molecular Biology of Yeast. Cold Spring Harbor, N.Y.: Cold Spring Harbor Laboratory, p. 164.

    Google Scholar 

  • Zubenko, G., Park, F., Jones, E. (1982). Genetic properties of mutations at the PEP4 locus in Saccharomyces cerevisiae. Genetics 102:679–690.

    PubMed  CAS  Google Scholar 

  • Zubenko, G., Park, F., Jones, E. (1983). Mutations in the PEP4 locus of Saccharomyces cerevisiae block the final step in the maturation of two vacuolar hydrolases. Proc. Natl. Acad. Sci. USA 80:510–514.

    Article  PubMed  CAS  Google Scholar 

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  1. Department of Biological Sciences, Carnegie-Mellon University, Pittsburgh, Pennsylvania, 15213, USA

    Elizabeth W. Jones

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    J. F. T. Spencer  & A. R. W. Smith  & 

  2. Goldsmith’ College, University of London, London, SE14 6NW, England

    Dorothy M. Spencer

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Jones, E.W. (1983). Genetic Approaches to the Study of Protease Function and Proteolysis in Saccharomyces cerevisiae . In: Spencer, J.F.T., Spencer, D.M., Smith, A.R.W. (eds) Yeast Genetics. Springer Series in Molecular Biology. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-5491-1_6

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