Intracellular Sorting and Processing of a Yeast Vacuolar Hydrolase: Proteinase A Propeptide Contains Vacuolar Targeting Information

LITERATURE CITED

• Ammerer, G., С. Р. Hunter, J. H. Rothman, G. C. Saari, L. A. Vails, and T. H. Stevens. 1986. PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar precursors. Mol. Cell. Biol. 6:2490–2499.
   PubMed Web of Science ®Google Scholar
• Ballou, С. 1982. Yeast cell wall and cell surface, p. 335–360. In J. Strathern, F. Jones, and T. Broach (ed.), The molecular biology of the yeast Saccharomyces: metabolism and gene expression. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Bankaitis, V. Α., L. M. Johnson, and S. D. Emr. 1986. Isolation of yeast mutants defective in protein targeting to the vacuole. Proc. Natl. Acad. Sci. USA 83:9075–9079.
   PubMed Web of Science ®Google Scholar
• Bedwell, D. M., D. J. Klionsky, and S. D. Emr. 1987. The yeast F1-ATPase β subunit precursor contains functionally redundant mitochondrial protein import information. Mol. Cell. Biol. 7:4038–4047.
   PubMedGoogle Scholar
• Blachly-Dyson, E., and T. H. Stevens. 1987. Yeast carboxypeptidase Y can be translocated and glycosylated without its amino-terminal signal sequence. J. Cell. Biol. 104:1183–1191.
   PubMed Web of Science ®Google Scholar
• Burger, M., E. Bacon, and J. Bacon. 1961. Some observations on the form and location of invertase in the yeast cell. Biochem. J. 78:504–511.
   PubMedGoogle Scholar
• Casadaban, M. J., and S. N. Cohen. 1980. Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J. Mol. Biol. 138:179–207.
   PubMed Web of Science ®Google Scholar
• Clark, D. W., J. S. Tkacz, and J. O. Lampen. 1982. Asparaginelinked carbohydrate does not determine the cellular location of yeast vacuolar nonspecific alkaline phosphatase. J. Bacteriol. 152:865–873.
   PubMedGoogle Scholar
• Clark, M. W., and J. Abelson. 1987. The subnuclear localization of tRNA ligase in yeast. J. Cell Biol. 105:1515–1526.
   PubMedGoogle Scholar
• Deshaies, R. J., and R. Schekman. 1987. A yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum. J. Cell Biol. 105:633–645.
   PubMedGoogle Scholar
• Emr, S. D., R. Schekman, M. C. Flessel, and J. Thoraer. 1983. An MFα1-SUC2 (α-factor-invertase) gene fusion for study of protein localization and gene expression in yeast. Proc. Natl. Acad. Sci. USA 80:7080–7084.
   PubMed Web of Science ®Google Scholar
• Goldstein, Α., and J. O. Lampen. 1975. β-D-Fructofuranoside fructohydrolase from yeast. Methods Enzymol. 42:504–511.
   PubMedGoogle Scholar
• Griffiths, F., and K. Simons. 1986. The trans Golgi network: sorting at the exit site of the Golgi complex. Science 234:438–443.
   PubMed Web of Science ®Google Scholar
• Hall, M. N., and A. D. Johnson. 1987. Horneo domain of the yeast repressor α2 is a sequence-specific DNA-binding domain but is not sufficient for repression. Science 237:1007–1012.
   PubMedGoogle Scholar
• Halvorson, H. O., and L. Ellias. 1958. The purification and properties of an α-glucosidase of Saccharomyces italicus Y1225. Biochim. Biophys. Acta 30:28–40.
   PubMed Web of Science ®Google Scholar
• Haselbeck, Α., and R. Schekman. 1986. Interorganelle transfer and glycosylation of yeast invertase in vitro. Proc. Natl. Acad. Sci. USA 83:2017–2021.
   PubMedGoogle Scholar
• Ηasilik, Α., and W. Tanner. 1976. Biosynthesis of carboxypep-tidase Y in yeast. Evidence for a precursor form of the glycoprotein. Biochem. Biophys. Res. Commun. 72:1430–1436.
   PubMedGoogle Scholar
• Hasilik, Α., and W. Tanner. 1978. Biosynthesis of the vacuolar yeast glycoprotein carboxypeptidase Y. Conversion of precursor into the enzyme. Eur. J. Biochem. 85:599–608.
   PubMedGoogle Scholar
• Hasilik, Α., and W. Tanner. 1978. Carbohydrate moiety of carboxypeptidase Y and perturbation of its synthesis. Eur. J. Biochem. 91:567–575.
   PubMedGoogle Scholar
• Hemmings, Β. Α., G. S. Zubenko, A. Hasilik, and E. W. Jones. 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.
   PubMed Web of Science ®Google Scholar
• James, M. N. G., and A. R. Sielecki. 1986. Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 Å resolution. Nature (London) 319:33–38.
   PubMed Web of Science ®Google Scholar
• Johnson, L. M., V. A. Bankaitis, and S. D. Emr. 1987. Distinct sequence determinants direct intracellular sorting and modification of a yeast vacuolar protease. Cell 48:875–885.
   PubMedGoogle Scholar
• Kaiser, C. Α., and D. Botstein. 1986. Secretion-defective mutations in the signal sequence for Saccharomvces cerevisiae invertase. Mol. Cell. Biol. 6:2382–2391.
   PubMed Web of Science ®Google Scholar
• Kaneko, Y., Y. Tamai, A. Toh-e, and Y. Oshima. 1985. Transcriptional and posttranscriptional control of PH08 expression by PHO regulatory genes in Saccharomvces cerevisiae. Mol. Cell. Biol. 5:248–252.
   PubMed Web of Science ®Google Scholar
• Kelly, R. B. 1985. Pathways of protein secretion in euckaryotes. Science 230:25–32.
   PubMed Web of Science ®Google Scholar
• Kubota, S., Y. Yoshida, H. Kumaoka, and A. Furumichi. 1977. Studies on the microsomal electron-transport system of anaero-bically grown yeast. J. Biochem. 81:197–206.
   PubMedGoogle Scholar
• Kuo, S. C., and J. O. Lampen. 1974. Tunicamycin, inhibitor of yeast glycoprotein synthesis. Biochem. Biophys. Res. Commun. 58:287–295.
   PubMed Web of Science ®Google Scholar
• Lenney, J., P. Matile, A. Wiemken, M. Schellenberg, and J. Meyer. 1974. Activities and cellular localization of yeast proteinases and their inhibitors. Biochem. Biophys. Res. Commun. 60:1378–1383.
   PubMed Web of Science ®Google Scholar
• Mage, M. G. 1980. Preparation of Fab fragments from IgGs of different animal species. Methods Enzymol. 70:142–150.
   PubMedGoogle Scholar
• Mechler, В., M. Müller, H. Müller, F. Meussdoerffer, and D. H. Wolf. 1982. In vivo biosynthesis of the vacuolar proteinases A and В in the yeast Saccharomvces cerevisiae. J. Biol. Chem. 257:11203–11206.
   PubMed Web of Science ®Google Scholar
• Mechler, В., M. Müller, H. Müller, and D. Wolf. 1982. In vivo biosynthesis of vacuolar proteinases in proteinase mutants of Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 107:770–778.
   PubMedGoogle Scholar
• Mechler, В., H. Müller, and D. H. Wolf. 1987. Maturation of vacuolar (lysosomal) enzymes in yeast: proteinase y sc A and proteinase yscB are catalysts of the processing and activation event of carboxypeptidase yscY. EMBO J. 6:2157–2163.
   PubMed Web of Science ®Google Scholar
• Messing, J., and J. Vieira. 1982. A new pair of M13 vectors for selecting either DNA strand of double-digest restriction fragments. Gene 19:269–276.
   PubMed Web of Science ®Google Scholar
• Miller, J. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Moehle, C. M., M. W. Aynardi, M. R. Kolodny, F. J. Park, and E. W. Jones. 1987. Protease В of Saccharomyces cerevisiae: isolation and regulation of the PRB1 structural gene. Genetics 115:255–263.
   PubMedGoogle Scholar
• Neuman, A. J., R.-J. Lin, S.-C. Cheng, and J. Abelson. 1985. Molecular consequences of specific intron mutations on yeast mRNA splicing in vivo and in vitro. Cell 42:335–344.
   PubMedGoogle Scholar
• Novick, P., C. Field, and R. Schekman. 1980. Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell 21:205–215.
   PubMed Web of Science ®Google Scholar
• Novick, P., and R. Schekman. 1979. Secretion and cell surface growth are blocked in a temperature-sensitive mutant of Saccharomvces cerevisiae. Proc. Natl. Acad. Sci. USA 76:1858–1862.
   PubMed Web of Science ®Google Scholar
• Onishi, H. R., J. S. Tkacz, and J. O. Lampen. 1979. Glycoprotein nature of yeast alkaline phosphatase. J. Biol. Chem. 254:11943–11952.
   PubMed Web of Science ®Google Scholar
• Opheim, D. J. 1978. α-D-Mannosidase of Saccharomyces cerevisiae characterization and modulation of activity. Biochim. Biophys. Acta 524:121–130.
   PubMedGoogle Scholar
• Perlman, D., P. Raney, and H. O. Halvorson. 1986. Mutations affecting the signal sequence alter synthesis and secretion of yeast invertase. Proc. Natl. Acad. Sci. USA 83:5033–5037.
   PubMedGoogle Scholar
• Preston, R. Α., R. F. Murphy, and E. W. Jones. 1987. Apparent endocytosis of fluorescein isothiocyanate-conjugated dextran by Saccharomyces cerevisiae reflects uptake of low molecular weight impurities, not dextran. J. Cell Biol. 105:1981–1987.
   PubMed Web of Science ®Google Scholar
• Richardson, W. D., B. L. Roberts, and A. E. Smith. 1986. Nuclear location signals in polyoma virus large-T. Cell 44:77–85.
   PubMedGoogle Scholar
• Riezman, H. 1985. Endocytosis in yeast: several of the yeast secretory mutants are defective in endocytosis. Cell 40:1001–1009.
   PubMedGoogle Scholar
• Rothman, J. H., C. P. Hunter, L. A. Vails, and T. H. Stevens. 1986. Overproduction-induced mislocalization of a yeast vacuolar protein allows isolation of its structural gene. Proc. Natl. Acad. Sci. USA 83:3248–3252.
   PubMedGoogle Scholar
• Rothman, J. H., and T. H. Stevens. 1986. Protein sorting in yeast: mutants defective in vacuole biogenesis mislocalize vacuolar proteins into the late secretory pathway. Cell 47:1041–1051.
   PubMed Web of Science ®Google Scholar
• Rothstein, R. J. 1983. One-step gene disruption in yeast. Methods Enzymol. 101:202–212.
   PubMed Web of Science ®Google Scholar
• Sanger, F., F. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463–5467.
   PubMed Web of Science ®Google Scholar
• Schwaiger, Η., A. Hasilik, K. von Figura, A. Wiemken, and W. Tanner. 1982. Carbohydrate-free carboxypeptidase Y is transferred into the lysosome-like yeast vacuole. Biochem. Biophys. Res. Commun. 104:950–956.
   PubMedGoogle Scholar
• Sherman, F., G. R. Fink, and C. W. Lawrence. 1979. Methods in yeast genetics: a laboratory manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Sly, W. S., and H. D. Fischer. 1982. The phosphomannosyl recognition system for intracellular and intercellular transport of lysosomal enzymes. J. Cell. Biochem. 18:67–85.
   PubMed Web of Science ®Google Scholar
• Stevens, Т., В. Esmon, and R. Schekman. 1982. Early stages in the yeast secretory pathway are required for transport of carboxypeptidase Y to the vacuole. Cell 30:439–448.
   PubMedGoogle Scholar
• Stevens, T. H., J. H. Rothman, G. S. Payne, and R. Schekman. 1986. Gene dosage-dependent secretion of yeast vacuolar carboxypeptidase Y. J. Cell Biol. 102:1551–1557.
   PubMedGoogle Scholar
• Trimble, R. В., and F. Maley. 1977. The use of endo-β-N-acetylglucosaminidase H in characterizing the structure and function of glycoproteins. Biochem. Biophys. Res. Commun. 78:935–944.
   PubMed Web of Science ®Google Scholar
• Trimble, R. В., F. Maley, and F. K. Chu. 1983. Glycoprotein biosynthesis in yeast. Protein conformation affects processing of high mannose oligosaccharides on carboxypeptidase Y and invertase. J. Biol. Chem. 258:2562–2567.
   PubMedGoogle Scholar
• Vails, L. Α., С. P. Hunter, J. H. Rothman, and T. H. Stevens. 1987. Protein sorting in yeast: the localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptide. Cell 48:887–897.
   PubMedGoogle Scholar
• von Heijne, G. 1986. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14:4683–4690.
   PubMed Web of Science ®Google Scholar
• Weisman, L. S., R. Bacallao, and W. Wickner. 1987. Multiple methods of visualizing the yeast vacuole permit evaluation of its morphology and inheritance during the cell cycle. J. Cell Biol. 105:1539–1547.
   PubMed Web of Science ®Google Scholar
• Wickerham, L. J. 1946. A critical evaluation of the nitrogen assimilation tests commonly used in the classification of yeasts. J. Bacteriol. 52:293–301.
   Google Scholar
• Wieland, F. T., M. L. Gleason, T. A. Serafini, and J. E. Rothman. 1987. The rate of bulk flow from the endoplasmic reticulum to the cell surface. Cell 50:289–300.
   PubMed Web of Science ®Google Scholar
• Wiemken, Α., M. Schellenberg, and K. Urech. 1979. Vacuoles: the sole compartments of digestive enzymes in yeast (Saccharomyces cerevisiae)! Arch. Microbiol. 123:23–35.
   Google Scholar
• Woolford, С. Α., L. B. Daniels, F. J. Park, E. W. Jones, J. N. van Arsdell, and M. A. Innis. 1986. The PEP4 gene encodes an aspartyl protease implicated in the posttranslational regulation of Saccharomvces cerevisiae vacuolar hydrolases. Mol. Cell. Biol. 6:2500–2510.
   PubMed Web of Science ®Google Scholar
• Zubenko, G. S., F. J. Park, and E. W. Jones. 1983. Mutations in PEP4 locus of Saccharomyces cerevisiae block final step in maturation of two vacuolar hydrolases. Proc. Natl. Acad. Sci. USA 80:510–514.
   PubMedGoogle Scholar