Summary
On the basis of genetic data it has been suggested that repressible acid phosphatase of Saccharomyces cerevisiae is regulated by a control circuit involving operator-repressor mechanisms (Toh-e et al., 1978).
We measured no significant difference in the amount of translatable mRNA of repressed and derepressed cells in the reticulocyte in vitro translation system. We find a 25 fold difference in specific enzyme activity in repressed versus derepressed cells whereas the amount of 25S-methionine labelled enzyme protein as measured by antibody precipitation varies only 2–3 fold. This argues for posttranslational regulation of preexisting inactive acid phosphatase. Minor regulatory effects at the transcriptional or translational level cannot be excluded.
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References
Boer, P., Steyn-Parvé, E.P.: Isolation and purification of an acid phosphatase from baker's yeast (Saccharomyces cerevisiae). Biochim. Biophys. Acta 128, 400–402 (1966)
Dibenedetto, G., Cozzani, I.: Nonspecific acid phosphatase from Schizosaccharomyces pombe. Purification and physical chemical properties. Biochemistry 14, 2847–2852 (1975)
Linnemans, W.A.M., Boer, P., Elbers, P.F.: Localization of acid phosphatase in Saccharomyces cerevisiae: a clue to cell wall for mation. J. Bacteriol. 131, 638–644 (1977)
Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J.: Protein measurement with the Folin phenol ragent. J. Biol. Chem. 193, 265–275 (1951)
Maurer, A.R., Stone, R., Gorski, I.: Cell-free synthesis of a large translation product of prolactin messenger RNA. J. Biol. Chem. 251, 2801–2807 (1976)
Mort, A.J., Lamport, D.T.A.: Anhydrous hydrogen fluoride deglycosylates glycoproteins. Anal. Biochem. 82, 289–309 (1977)
Palmiter, D.R., Oka, T., Schimke, R.T.: Modulation of ovalbumin synthesis by estradiol-17 β and actinomycin D as studied in explants of chick oviduct in culture. J. Biol. Chem. 246, 724–737 (1971)
Rice, R.H., Means, G.E.: Radioactive labelling of proteins in vitro. J. Biol. Chem. 246, 831–832 (1971)
Rubin, G.M.: The nucleotide sequence of Saccharomyces cerevisiae 5.8 s ribosomal ribonucleic acid. J. Biol. Chem. 248, 3860–3875 (1973)
Schurr, A., Yagil, E.: Regulation and characterization of acid and alkaline phosphatase in yeast. J. Gen Microbiol. 65, 291–303 (1971)
Toh-e, A., Kakimoto, S., Oshima, Y.: Genes coding for the structure of the acid phosphatase in Saccharomyces cerevisiae. Mol. Gen. Genet. 143, 65–70 (1975)
Toh-e, A., Kobayashi, S., Oshima, Y.: Disturbance of the machinery for the gene expression by acidic pH in the repressible acid phosphatase system of Saccharomyces cerevisiae. Mol. Gen. Genet. 162, 139–149 (1978)
Toh-e, A., Nakamura, H., Oshima, Y.: A gene controlling the synthesis of non specific alkaline phosphatase in Saccharomyces cerevisiae. Biochim. Biophys. Acta 428, 182–192 (1976)
Toh-e, A., Oshima, Y.: Characterization of a dominant, constitutive mutation, PHOO, in the repressible acid phosphatase synthesis in Saccharomyces cerevisiae. J. Bacteriol. 120, 608–617 (1974)
Toh-e, A., Ueda, Y., Kakimoto, S., Oshima, Y.: Isolation and characterization of acid phosphatase mutants in Saccharomyces cerevisiae. J. Bacteriol. 113, 727–738 (1973)
Trimble, R.B., Maley, F.: Subunit structure of external invertase from Saccharomyces cerevisiae. J. Biol. Chem. 252, 4409–4412 (1977)
Ueda, Y., Toh-e, A., Oshima, Y.: Isolation and characterization of recessive, constitutive mutants for repressible acid phosphatase synthesis in Saccharomyces cerevisiae. J. Bacteriol. 122, 911–922 (1975)
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Communicated by F. Kaudewitz
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Schweingruber, M.E., Schweingruber, AM. Posttranslational regulation of repressible acid phosphatase in yeast. Molec. Gen. Genet. 173, 349–351 (1979). https://doi.org/10.1007/BF00268647
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DOI: https://doi.org/10.1007/BF00268647