1887

Abstract

SUMMARY: The turnover of protein in a prototrophic strain of Bacillus stearothermophilus during exponential growth in a salts medium with glucose or succinate as carbon source was about 4 %/h and in a richer nutrient broth medium about 23 %/h. Protein degradation under non-growing conditions conformed to a similar pattern. The turnover of RNA (non-messenger) was about 1 %/h in salts medium and about 9 %/h in nutrient broth. The turnover of protein and RNA in the thermophile is thus moderate rather than massive. This conclusion was confirmed by measurement of the decay of a specific enzyme, isocitrate lyase, in the proto-troph and of the overall protein turnover in a non-prototrophic strain of . The half-lives of a number of enzyme systems in intact cells of the prototrophic thermophile at its optimum growth temperature showed some variation but indicated a significant rate of inactivation. Such decay of protein in vivo apparently accounts for the moderate protein turnover observed during growth.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-91-2-383
1975-12-01
2021-05-13
Loading full text...

Full text loading...

/deliver/fulltext/micro/91/2/mic-91-2-383.html?itemId=/content/journal/micro/10.1099/00221287-91-2-383&mimeType=html&fmt=ahah

References

  1. Allen M. B. 1953; The thermophilic aerobic sporeforming bacteria. Bacteriological Reviews. 24:289–308
    [Google Scholar]
  2. Amelunxen R., Lins M. 1968; Comparative thermostability of enzymes fromBacillus stearothermophilus.andBacillus cereus. . Archives of Biochemistry and Biophysics. 125:765–769
    [Google Scholar]
  3. Brock T. D. 1967; Life at high temperatures. Science; New York: 1581012–1019
    [Google Scholar]
  4. Bubela B., Holdsworth E. S. 1966; Amino acid uptake, protein and nucleic acid synthesis and turnover inBacillus stearothermophilus. . Biochimica et biophysica acta. 123:364–375
    [Google Scholar]
  5. Bucher T., Pfleiderer G. 1955; Pyruvate kinase from muscle. Methods in Enzymology. 1:435–440
    [Google Scholar]
  6. Cazzulo J. J., Sundaram T. K., Kornberg H. L. 1969; Regulation of pyruvate carboxylase formation from the apoenzyme and biotin in a thermophilic Bacillus. Nature London: 223:1137–1138
    [Google Scholar]
  7. Cazzulo J. J., Sundaram T. K., Kornberg H. L. 1970; Properties and regulation of pyruvate carboxylase fromBacillus stearothermophilus. . Proceedings of the Royal Society. B176:1–19
    [Google Scholar]
  8. Coultate T. P., Sundaram T. K. 1975; Energetics ofBacillus stearothermophilus.growth: molar growth yield and temperature effects on growth efficiency. Journal of Bacteriology. 121:55–64
    [Google Scholar]
  9. Epstein I., Grossowicz N. 1969a; Prototrophic thermophilic bacillus. Isolation, properties and kinetics of growth. Journal of Bacteriology. 99:414–417
    [Google Scholar]
  10. Epstein I., Grossowicz N. 1969b; Intracellular protein breakdown in a thermophile. Journal of Bacteriology. 99:418–421
    [Google Scholar]
  11. Goldberg A. L., Dice J. F. 1974; Intracellular protein degradation in mammalian and bacterial cells. Annual Review of Biochemistry. 43:835–869
    [Google Scholar]
  12. Griffiths M. W., Sundaram T. K. 1973; Isocitrate lyase from a thermophilicBacillus.: effect of salts on enzyme activity. Journal of Bacteriology. 116:1160–1169
    [Google Scholar]
  13. Halvorson H. O. 1962; The function and control of intracellular protein turnover in microorganisms. In Amino Acid Pools pp. 646–654 Holden J. T. Edited by Amsterdam: Elsevier;
    [Google Scholar]
  14. Kornberg H. L. 1965; Control of biosynthesis from C2compounds. In Mecanismes de regulation des activites cellulaires chez les microorganismes. Colloques Internationaux du Centre National de la Recherche Scientifique. 124: pp. 193–207
    [Google Scholar]
  15. Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. 1951; Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry. 193:265–275
    [Google Scholar]
  16. Mandelstam J. 1960; The intracellular turnover of protein and nucleic acids and its role in biochemical differentiation. Bacteriological Reviews. 24:289–308
    [Google Scholar]
  17. Mandelstam J., Waites W. M. 1968; Sporulation inBacillus subtilis.The role of exoprotease. Biochemical Journal. 109:793–801
    [Google Scholar]
  18. Ochoa S. 1955; Malic dehydrogenase from pig heart. Methods in Enzymology. 1:735–739
    [Google Scholar]
  19. Pine M. J. 1972; Turnover of intracelluar proteins. Annual Review of Microbiology 26103–126
    [Google Scholar]
  20. Schimke R. T. 1969; On the roles of synthesis and degradation in regulation of enzyme levels in mammalian tissues. In Current Topics in Cellular Regulation 1 pp. 77–124 Horecker B. L., Stadtman E. R. Edited by New York and London: Academic Press;
    [Google Scholar]
  21. Self C. H., Weitzman P. D. J. 1970; Separation of isoenzymes by zonal centrifugation. Nature; London: 225644–645
    [Google Scholar]
  22. Sundaram T. K. 1973; Physiological role of pyruvate carboxylase in a thermophilic bacillus. Journal of Bacteriology. 113:549–557
    [Google Scholar]
  23. Sundaram T. K., Cazzulo J. J., Kornberg H. L. 1971; Synthesis of pyruvate carboxylase from its apoenzyme and (+)-biotin inBacillus stearothermophilus.Mechanism and control of the reaction. Biochemical Journal. 122:663–669
    [Google Scholar]
  24. Tarver H. 1954; Peptide and protein synthesis: protein turnover. In The Proteins 2B pp. 1199–1296 Neurath H., Bailey K. C. Edited by New York: Academic Press;
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-91-2-383
Loading
/content/journal/micro/10.1099/00221287-91-2-383
Loading

Data & Media loading...

Most cited this month Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error