1887

Abstract

Proteolytic activities, active against casein and insulin are present in cell-free extracts of the psychrotrophic bacterium S55. These activities were compared (i) following growth of the bacterium at different temperatures (10, 20 and 32C) and (ii) after a temperature shift from 10 to 32C. Both activities (measured at 20C) were greater in cells grown at 32C and after a temperature shift. Chloramphenicol prevented the increases in activities. The proteolysis of casein was stimulated by ATP; the stimulation was greater following a temperature shift. In addition, proteolysis of casein (measured at 20C) was activated by pre-incubation at temperatures between 45 and 60C; the proportion of proteolytic activity activated by such treatment also increased with growth temperature. Comparison by two-dimensional electrophoresis of the polypeptides synthesized at 10 and 32C suggests that S55 produces proteins specific to both temperatures (13 species were either exclusive to or present in increased amounts during growth at 10C, while at least 21 polypeptides were preferentially synthesized at 32C). A temperature shift from 10 to 32C promoted the synthesis of at least 16 polypeptides, many with values similar to those of heat shock proteins synthesized at higher temperatures in mesophiles. A temperature up-shift of S55 from 10 to 20C did not provoke the synthesis of new proteins; heat shock proteins were produced only at 28C and higher. The similarity in kinetics of the appearance of heat shock proteins and the increase in proteolytic activities suggest that in S55 some heat shock proteins might also possess protein catabolic function.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-136-2-283
1990-02-01
2024-12-09
Loading full text...

Full text loading...

/deliver/fulltext/micro/136/2/mic-136-2-283.html?itemId=/content/journal/micro/10.1099/00221287-136-2-283&mimeType=html&fmt=ahah

References

  1. Anathan J., Goldberg A. L., Voellmy R. 1986; Abnormal proteins serve as eukaryotic stress signal and trigger the activation of heat shock genes. Science 232:522–524
    [Google Scholar]
  2. Burton J. 1951; A study of the conditions and mechanisms of the diphenylamine reaction of the colorimetric estimation of deoxyribonucleic acid. Biochemical Journal 162:315–323
    [Google Scholar]
  3. Chesshyre J. A., Hipkiss A. R. 1989; Low temperature stabilizes interferon a-2 against proteolysis in Methylophilus methylotrophus and Escherichia coli. . Applied Microbiology and Biotechnology 31:158–162
    [Google Scholar]
  4. Chung C. H., Goldberg A.L. 1981; The product of the Ion (capR) gene in Escherichia coli is the ATP-dependente protease La. Proceedings of the National Academy of Sciences of the United States of America 78:4931–4935
    [Google Scholar]
  5. Craig E. A. 1985; The heat shock response. Critical Reviews in Biochemistry 18:239–280
    [Google Scholar]
  6. Davis B. D., Tal P. C. 1980; The mechanism of protein secretion across membranes. Nature, London 283:433–438
    [Google Scholar]
  7. Goff S. A., Casson L. P., Goldberg A. L. 1984; The heat shock regulatory gene htpR influences rates of protein degradation and expression of the Ion gene in Escherichia coli. . Proceedings of the National Academy of Sciences of the United States of America 81:6647–6651
    [Google Scholar]
  8. Goff S. A., Goldberg A. L. 1985; Production of abnormal proteins in Escherichia coli stimulates transcription of Ion and other heat shock genes. Cell 41:587–595
    [Google Scholar]
  9. Goff S. A., Goldberg A. L. 1987; An increased content of protease La, the Ion gene product, increases protein degradation and blocks growth in Escherichia coli. . Journal of Biological Chemistry 262:4508–4515
    [Google Scholar]
  10. Goldberg A. L. 1972; Degradation of abnormal proteins in Escherichia coli. . Proceedings of the National Academy of Sciences of the United States of America 69:422–426
    [Google Scholar]
  11. Goldberg A. L., St John A. C. 1976; Intracellular protein degradation in mammalian and bacterial cells (2). Annual Review of Biochemistry 45:747–803
    [Google Scholar]
  12. Gounot A. M. 1976; Effects of temperature on the growth of the psychrophilic bacteria from glaciers. Canadian Journal of Microbiology 22:357–362
    [Google Scholar]
  13. Ichihara S., Beppu N., Mizushima S. 1984; Protease IV, a cytoplasmic protein of Escherichia coli, has signal peptide peptidase activity. Journal of Biological Chemistry 259:9853–9857
    [Google Scholar]
  14. Kelly P. M., Schlesinger M. J. 1978; The effect of amino acid analogues and heat shock on gene expression in chicken embryo fibroblast. Cell 15:1277–1286
    [Google Scholar]
  15. Laemmli U. K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, Jjondon 227:680–685
    [Google Scholar]
  16. Mccallum K. L., Heikkila J. J., Inniss W. E. 1986; Temperature-dependent pattern of heat-shock protein synthesis in psychrophilic and psychrotrophic microorganisms. Canadian Journal of Microbiology 32:516–521
    [Google Scholar]
  17. Mandelstam J. 1963; Protein turnover and its function in the economy of the cell. Annals of the New York Academy of Sciences 102:621–636
    [Google Scholar]
  18. Morita R. Y. 1975; Psychrophilic bacteria. Bacteriological Reviews 39:144–167
    [Google Scholar]
  19. Mosteller R. D., Goldstein R. V., Nishimoto K. R. 1980; Metabolism of individual proteins in exponentially growing Escherichia coli. . Journal of Biological Chemistry 255:2524–2532
    [Google Scholar]
  20. Munro S., Pelham H. 1985 What turns on heat shock genes? Nature, London 317:477–478
    [Google Scholar]
  21. Neidhardt F. C., Vanbogelen R. A., Vaughn V. 1984; The genetics and regulation of heat-shock proteins. Annual Review of Genetics 18:295–329
    [Google Scholar]
  22. Neidhardt F. C., Vanbogelen R. A. 1987; Heat shock response. In Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology pp 1334–1345 Neidhardt F. C., Ingraham J. L., Low K. B., Magasanik B., Schaechter M., Umbarger H. E. Edited by Washington, DC: American Society for Microbiology;
    [Google Scholar]
  23. O’Farrell P. H. 1975; High resolution two-dimensional electrophoresis of proteins. Journal of Biological Chemistry 250:4007–4021
    [Google Scholar]
  24. Phillips T. A., Vanbogelen R. A., Neidhardt F. C. 1984; Ion gene product of Escherichia coli is a heat-shock protein. Journal of Bacteriology 159:283–287
    [Google Scholar]
  25. Potier P., Hipkiss A. R., Kushner D. J. 1985; Protein turnover in a psychrotrophic bacterium. Archives of Microbiology 142:28–33
    [Google Scholar]
  26. Potier P., Drevet P., Gounot A. M., Hipkiss A. R. 1987a; Protein turnover in a psychrotrophic bacterium: proteolytic activity in extracts of cells grown at different temperatures. FEMS Microbiology tetters 44:267–271
    [Google Scholar]
  27. Potier P., Drevet P., Gounot A. M., Hipkiss A. R. 1987b; ATP-dependent and -independent protein degradation in extracts of the psychrotophic bacterium Arthrobacter sp. St55. Journal of General Microbiology 133:2797–2806
    [Google Scholar]
  28. Potier P., Drevet P., Gounot A. M., Hipkiss A. R. 1987; c)Proteolysis in cell-free extracts of the psychrophilic (cold-loving) bacterium Arthrobacter sp. Si 55: effects of growth temperature and ATP. Biochemical Society Transactions 15:968–969
    [Google Scholar]
  29. Rice R. H., Means G. E. 1970; Radioactive labelling of proteins in vitro. . Journal of Biological Chemistry 246:831–832
    [Google Scholar]
  30. Straus D. B., Walter W. A., Gross C. A. 1988; Escherichia coli heat shock gene mutants are defective in proteolysis. Genes and Development 2:1851–1858
    [Google Scholar]
  31. Yamamori T., Ito K., Nakamura Y., Yura T. 1978; Transient regulation of protein synthesis in Escherichia coli upon shift-up of growth temperature. Journal of Bacteriology 134:1133–1140
    [Google Scholar]
/content/journal/micro/10.1099/00221287-136-2-283
Loading
/content/journal/micro/10.1099/00221287-136-2-283
Loading

Data & Media loading...

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