Skip to main content
SpringerLink
Log in

A bacterial inhibitor of animal protein kinases

  • Published:
Current Microbiology Aims and scope Submit manuscript

Abstract

Cellular extracts ofEscherichia coli severely impair the protein-phosphorylating activity in vitro of animal enzymes of both the casein-kinase type and the histone-kinase type. This blockade is due to a protein, probably dimeric, acting as a noncompetitive inhibitor, which has been purified to near-homogeneity from the soluble fraction of bacterial cells by chromatographic procedures.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

Literature Cited

  1. Abdel-Ghany M, Raden D, Racker E, Katchalski-Katzir E (1988) Phosphorylation of synthetic random polypeptides by protein kinase P and other protein-serine (threonine) kinases and stimulation or inhibition of kinase activities by microbial toxins. Proc Natl Acad Sci USA 85:1408–1411

    Google Scholar 

  2. Blobel G, Sabatini DD (1970) Controlled proteolysis of nascent polypeptides in rat liver cell fractions. I. Location of the polypeptides within ribosomes. J Cell Biol 45:130–145

    Google Scholar 

  3. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem 72:248–254

    Google Scholar 

  4. Cenatiempo Y, Cozzone AJ, Genot A, Reboud JP (1978) Characterization of two distinct protein kinase activities bound to membrane-free rat liver polysomes. Biochimie 60:813–816

    Google Scholar 

  5. Cozzone AJ (1988) Protein phosphorylation in prokaryotes. Annu Rev Microbiol 42:97–125

    Google Scholar 

  6. Dadssi M, Cozzone AJ (1990) Occurrence of protein phosphorylation in various bacterial species. Int J Biochem 22:493–499

    Google Scholar 

  7. Dadssi M, Cenatiempo Y, Cozzone AJ (1982) Further analysis of the polysomal casein kinase activity of rat liver. Mol Biol Rep 8:85–90

    Google Scholar 

  8. Dadssi M, Duclos B, Cozzone AJ (1989) A peptide substrate forEscherichia coli protein kinase activity in vitro. Biochem Biophys Res Commun 160:552–558

    Google Scholar 

  9. Garnak M, Reeves HC (1978) Phosphorylation of isocitrate dehydrogenase ofEscherichia coli. Science 203:1111–1112

    Google Scholar 

  10. Garnak M, Reeves HC (1979) Purification and properties of phosphorylated isocitrate dehydrogenase ofEscherichia coli. J Biol Chem 254:7915–7920

    Google Scholar 

  11. Gordon J (1971) Determination of an upper limit to the phosphorus content of polypeptide chain elongation factor and ribosomal proteins inEscherichia coli. Biochem Biophys Res Commun 44:579–586

    Google Scholar 

  12. Khandelwal RL, Spearman TN, Hamilton IR (1973) Protein kinase activity in cariogenic and non-cariogenic oral streptococci: activation and inhibition by cyclic AMP. FEBS Lett 31:246–250

    Google Scholar 

  13. Kuo JF, Greengard P (1969) An adenosine 3′–5′-monophosphate-dependent protein kinase fromEscherichia coli. J Biol Chem 244:3417–3419

    Google Scholar 

  14. Kurek E, Grankowski N, Gasior E (1972) On the phosphorylation ofEscherichia coli ribosomes. II. Reaction in cell-free system. Acta Microbiol Pol 4:177–183

    Google Scholar 

  15. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685

    Google Scholar 

  16. Li HC, Brown GG (1973) Orthophosphate and histone dependent polyphosphate kinase fromE. coli. Biochem Biophys Res Commun 53:875–881

    Google Scholar 

  17. Manaï M, Cozzone AJ (1979) Analysis of the protein kinase activity ofEscherichia coli cells. Biochem Biophys Res Commun 91:819–826

    Google Scholar 

  18. Manaï M, Cozzone AJ (1979) Mise en évidence d'une activité protéine-kinase chezEscherichia coli. C R Seances Acad Sci III 289:367–370

    Google Scholar 

  19. Manaï M, Duclos B, Cozzone AJ (1984) Inhibitory effect of bacterial extracts on the activityin vitro of eukaryotic histone kinase. FEMS Microbiol Lett 23:319–323

    Google Scholar 

  20. Pastan I, Adhya S (1976) Cyclic adenosine 5′-monophosphate inEscherichia coli. Bacteriol Rev 40:527–551

    Google Scholar 

  21. Rahmsdorf HJ, Pai SH, Ponta H, Herrlich P, Roskoski R, Schweiger M, Studier FW (1974) Protein kinase induction inEscherichia coli by bacteriophage T7. Proc Natl Acad Sci USA 71:586–589

    Google Scholar 

  22. Saier MH, Wu LF, Reizer J (1990) Regulation of bacterial physiological processes by three types of protein phosphorylating systems. Trends Biochem Sci 15:391–395

    Google Scholar 

  23. Scott JD, Fischer EH, Takio K, Demaille JG, Krebs EH (1985) Amino acid sequence of the heat-stable inhibitor of the cAMP-dependent protein kinase from rabbit skeletal muscle. Proc Natl Acad Sci USA 82:5732–5736

    Google Scholar 

  24. Wang JYJ, Koshland DE (1978) Evidence for protein kinase activities in the prokaryoleSalmonella typhimurium. J Biol Chem 253:7605–7608

    Google Scholar 

  25. Wise BC, Glass DB, Chou CHJ, Raynor RL, Katoh N, Schatzman RS, Turner RS, Kibler RF, Kuo JF (1982) Phospholipid-sensitive Ca2+-dependent protein kinase from heart. II. Substrate specificity and inhibition by various agents. J Biol Chem 257:8489–8495

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Institut de Biologie et Chimie des Protéines, C.N.R.S., Université de Lyon, 69622, Villeurbanne, France

    Mustapha Dadssi &  Alain J. Cozzone

Authors
  1. Mustapha Dadssi
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Alain J. Cozzone
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Dadssi, M., Cozzone, A.J. A bacterial inhibitor of animal protein kinases. Current Microbiology 24, 207–211 (1992). https://doi.org/10.1007/BF01579283

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01579283

Keywords

Search

Navigation