Localization of Dipeptidyl Aminopeptidase yscIV in the Plasma Membrane of Free

Abstract

The subcellular distribution of dipeptidyl aminopeptidase activity was studied in protoplast lysates of that were virtually free from vacuolar contamination. Dipeptidyl aminopeptidase yscIV, the gene product, was found to be associated with plasma membrane vesicles after sucrose gradient isopycnic centrifugation. Another dipeptidyl aminopeptidase activity, not yet fully characterized, was localized in a microvesicular population co-sedimenting with chitosomes.

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1990-03-01
2024-03-29
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References

  1. Aibara S., Hayashi R., Hata T. 1971; Physical and chemical properties of yeast proteinase C. Agricultural and Biological Chemistry 35:658–666
    [Google Scholar]
  2. Boller T., Dürr M., Wiemken A. 1976; Asymmetric distribution of concanavalinA binding sites on yeast plasmalemma and vacuolar membrane. Archives of Microbiology 109:115–118
    [Google Scholar]
  3. Bordallo C., Schwencke J., Suárez-Rendueles M. P. 1984; Localization of the thermosensitive X-prolyldipeptidylaminopeptidase in the vacuolar membrane of Saccharomyces cerevisiae. FEBS Letters 173:199–203
    [Google Scholar]
  4. Bracker C. E., Ruiz-Herrera J., Bartnicki-García S. 1976; Structure and conformation of chitin synthetase particles (chitosomes) during microfibril synthesis in vitro. Proceedings of the National Academy of Sciences of the United States of America 73:4570–4574
    [Google Scholar]
  5. Bradford M. M. 1976; A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72:248–254
    [Google Scholar]
  6. Flores Martínez A., Schwencke J. 1988; Chitin synthetase activity is bound to chitosomes and to the plasma membrane in protoplasts of Saccharomyces cerevisiae. Biochimica et Biophysica Acta 946:328–336
    [Google Scholar]
  7. García-Alvarez N., Bordallo C., Gascón S., Suàrez-Rendueles M. P. 1985; Purification and characterization of a thermosensitive X-prolyl dipeptidyl aminopeptidase (dipeptidyl aminopeptidase yscV) from Saccharomyces cerevisiae. Biochimica et Biophysica Acta 832:119–125
    [Google Scholar]
  8. García-Ramos C., Cruz Camarillo R., Gascón S., Suàrez-Rendueles M. P. 1983; Studies on the regulation of X-prolyl dipeptidyl aminopeptidase activity. Journal of General Microbiology 129:3519–3523
    [Google Scholar]
  9. Hirsch H. H., Suàrez-Rendueles P., Wolf D. H. 1989; Yeast Saccharomyces cerevisiae proteinases.Structure, characteristics and function. In The Molecular and Cell Biology of Yeasts, pp 134–200 Walton E. F., Yarranton G. T. Edited by Glasgow: Blackie;
    [Google Scholar]
  10. Julius D., Blair L., Brake A., Sprague G., Thorner J. 1983; Yeast α-factor is processed from a larger precursor polypeptide: the essential role of a membrane-bound dipeptidyl aminopeptidase. Cell 32:839–852
    [Google Scholar]
  11. Julius D., Schekman R., Thorner J. 1984; Glycosylation and processing of prepro-α-factor through the yeast secretory pathway. Cell 36:309–318
    [Google Scholar]
  12. Opheim D. S. 1978; α-Mannosidase of Saccharomyces cerevisiae. Characterization and modulation of activity. Biochimica et Biophysica Acta 524:121–130
    [Google Scholar]
  13. Ruiz-Herrera J., Bartnicki-García S. 1976; Proteolytic activation and inactivation of chitin synthetase from Mucor rouxii. Journal of General Microbiology 97:241–249
    [Google Scholar]
  14. Ruiz-Herrera J., Bracker C. E., Bartnicki-García S. 1984; Sedimentation properties of chitosomes from Mucor rouxii. Protoplasma 122:176–190
    [Google Scholar]
  15. Scarborough G. A. 1975; Isolation and characterization of Neurospora crassa plasma-membrane. Journal of Biological Chemistry 250:1106–1111
    [Google Scholar]
  16. Schwencke J., Canut H., Flores A. 1983; Simultaneous isolation of the yeast cytosol and well-preserved mitochondria with negligible contamination by vacuolar proteinases. FEBS Letters 156:274–280
    [Google Scholar]
  17. Sprague G. F. JR Rine J., Herskowitz I. 1981; Control of yeast cell type by the mating type locus. II. Genetic interactions between MAT and unlinked α-specific STE genes. Journal of Molecular Biology 153:323–335
    [Google Scholar]
  18. Suàrez-Rendueles P., Wolf D. H. 1987; Identification of the structural gene for dipeptidylaminopeptidaeyscV (DAP2) of Saccharomyces cerevisiae. Journal of Bacteriology 169:4041–4048
    [Google Scholar]
  19. Suàrez-Rendueles M. P., Wolf D. H. 1988; Proteinase function in yeast: biochemical and genetic approaches to a central mechanism of post-translational control in the eukaryotic cell. FEMS Microbiology Reviews 54:17–46
    [Google Scholar]
  20. Suàrez-Rendueles M. P., Schwencke J., García-Alvarez N., Gascón S. 1981; A new X-prolyl dipeptidyl aminopeptidase from yeast associated with a particulate fraction. FEBS Letters 131:296–300
    [Google Scholar]
  21. Tanaka K., Yoshimura T., Kumatori A., Ichihara A., Ikai A., Nishigai M., Kameyama K., Takagi T. 1988; Proteasomes (multi-protease complexes) as 20 S ring-shaped particles in a variety of eukaryotic cells. Journal of Biological Chemistry 263:16209–16217
    [Google Scholar]
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