Folia Microbiologica

, Volume 42, Issue 3, pp 165–170 | Cite as

Diversity and specificity of protein-phosphorylating systems in bacteria

  • A. J. Cozzone
Papers
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Abstract

Bacteria harbor three different protein-phosphorylating systems which regulate distinct physiological processes: first, the nucleotide-dependent system which modifies hydroxyl groups of amino acids in protein substrates; second, the two-component system which involves both sensor kinase and response regulator; third, the phosphoenolpyruvate-dependent phosphotransferase system. These systems share a number of structural and functional similarities with the protein-phosphorylating systems of eukaryotes.

Keywords

Protein Phosphorylation Isocitrate Dehydrogenase Phosphoryl Group Rabbit Skeletal Muscle Sensor Kinase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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References

  1. Barker S., Matthews R., Lee W., Bostock A., Burnie J.:J. Med. Vet. Mycol. 29, 381–386 (1991).PubMedCrossRefGoogle Scholar
  2. Bourret R.B., Borkovich K.A., Simon M.I.:Ann. Rev. Biochem. 60, 401–441 (1991).PubMedCrossRefGoogle Scholar
  3. Chang C., Kwok S.F., Bleecker A.B., Meyerowitz E.M.:Science 262, 539–544 (1993).PubMedCrossRefGoogle Scholar
  4. Chiang T.M., Reizer J., Beachey E.H.:J. Biol. Chem. 264, 2957–2962 (1989).PubMedGoogle Scholar
  5. Cortay J.C., Duclos B., Cozzone A.J.:J. Mol. Biol. 187, 305–308 (1986a).PubMedCrossRefGoogle Scholar
  6. Cortay J.C., Rieul C., Duclos B., Cozzone A.J.:Eur. J. Biochem. 159, 227–237 (1986b).PubMedCrossRefGoogle Scholar
  7. Cortay J.C., Nègre D., Scarabel M., Ramseier T.M., Vartak N.B., Reizer J., Saier M.H., Cozzone A.J.:J. Biol. Chem. 269, 14885–14891 (1994).PubMedGoogle Scholar
  8. Cozzone A.J.:Ann. Rev. Microbiol. 42, 97–125 (1988).CrossRefGoogle Scholar
  9. Cozzone A.J.:J. Cell. Biochem. 51, 7–13 (1993).PubMedCrossRefGoogle Scholar
  10. Dadssi M., Cozzone A.J.:J. Biol. Chem. 265, 20996–20999 (1990).PubMedGoogle Scholar
  11. Deutscher J., Fischer C., Charrier V., Galinier A., Lindner C.:Folia Microbiol. 42, 171–178 (1997).CrossRefGoogle Scholar
  12. Duclos B., Grangeasse C., Vaganay E., Riberty M., Cozzone A.J.:J. Mol. Biol. 259, 891–895 (1996).PubMedCrossRefGoogle Scholar
  13. Edelman A.M., Blumenthal D.K., Krebs E.G.:Ann. Rev. Biochem. 56, 567–613 (1987).PubMedGoogle Scholar
  14. Fakunding J.L., Traugh J.A., Traut R.R., Hershey J.W.B.:J. Biol. Chem. 247, 6365–6367 (1972).PubMedGoogle Scholar
  15. Fantl W.J., Johnson D.E., Williams L.T.:Ann. Rev. Biochem. 62, 453–481 (1993).PubMedGoogle Scholar
  16. Freestone P., Grant S., Toth I., Norris V.:Molec. Microbiol. 15, 573–580 (1995).CrossRefGoogle Scholar
  17. Galyov E.E., Hakansson S., Wolf-Watz H.:J. Bacteriol. 176, 4543–4548 (1994).PubMedGoogle Scholar
  18. Garnak M., Reeves H.C.:Science 203, 1111–1112 (1979).PubMedCrossRefGoogle Scholar
  19. Hunter T.:Cell 80, 225–236 (1995).PubMedCrossRefGoogle Scholar
  20. Hunter T.:Methods Enzymol. 200, 3–37 (1991).PubMedGoogle Scholar
  21. Janeček J., Moravec V., Dobrová Z., Janda I., Weiser J.:FEMS Microbiol. Lett. 133, 91–94 (1995).CrossRefGoogle Scholar
  22. Krebs E.G., Fischer E.H.:Biochim. Biophys. Acta 20, 150–157 (1956).PubMedCrossRefGoogle Scholar
  23. Laporte D.C., Stueland C.S., Ikeda T.:Biochimie 71, 1051–1057 (1989).PubMedCrossRefGoogle Scholar
  24. Manai M., Cozzone A.J.:Biochem. Biophys. Res. Commun. 91, 819–826 (1979).PubMedGoogle Scholar
  25. Matsumoto A., Hong S.K., Ishizuka H., Horinouchi S., Beppu T.:Gen 146, 47–56 (1994).CrossRefGoogle Scholar
  26. Norris V., Baldwin T.J., Sweeney S.T., Williams P.H., Leach K.L.:Molec. Microbiol. 5, 2977–2983 (1991).CrossRefGoogle Scholar
  27. Oda K., Hasunuma K.:FEBS Lett. 345, 162–166 (1994).PubMedCrossRefGoogle Scholar
  28. Ota I.M., Varshavsky A.:Science 262, 566–569 (1993).PubMedCrossRefGoogle Scholar
  29. Parkinson J.S., Kofoid E.C.:Ann. Rev. Genet. 26, 71–112 (1992).PubMedCrossRefGoogle Scholar
  30. Parkinson J.S.:Cell 73, 857–871 (1993).PubMedCrossRefGoogle Scholar
  31. Postma P.W., Lengeler J.W., Jacobson G.R.:Microbiol. Rev. 57, 543–594 (1993).PubMedGoogle Scholar
  32. Rahmsdorf H.J., Pai S.H., Ponta H., Herrlich P., Roskoski R.:Proc. Nat. Acad. Sci. USA 71, 586–589 (1974).PubMedCrossRefGoogle Scholar
  33. Ranjeva R., Boudet A.M.:Ann. Rev. Plant Physiol. 38, 79–93 (1987).Google Scholar
  34. Saier M.H., Chauvaux S., Deutscher J., Reizer J., Ye J.J.:Trends Biochem. Sci. 20, 267–271 (1995).PubMedCrossRefGoogle Scholar
  35. Saier M.H., Wu L.F., Reizer J.:Trends Biochem. Sci. 15, 391–395 (1990).PubMedCrossRefGoogle Scholar
  36. Segovia M., Vicente C.:J. Plant Physiol. 146, 437–444 (1995).Google Scholar
  37. Seror S.J., Casaregola S., Vannier F., Zouari N., Dahl M., Boye E.:EMBO J. 13, 2472–2480 (1994).PubMedGoogle Scholar
  38. Stock J.B., Ninfa A.J., Stock A.M.:Microbiol. Rev. 53, 450–490 (1989).PubMedGoogle Scholar
  39. Traugh J.A., Traut R.R.:Biochemistry 11, 2503–2509 (1972).PubMedCrossRefGoogle Scholar
  40. Wang J.Y., Koshland D.E.:J. Biol. Chem. 253, 7605–7608 (1978).PubMedGoogle Scholar
  41. Wanner B.L.:J. Bacteriol. 174, 2053–2058 (1992).PubMedGoogle Scholar
  42. Zhang C.C.:Proc. Nat. Acad. Sci. USA 90, 11840–11844 (1993).PubMedCrossRefGoogle Scholar
  43. Zhang W., Munoz-Dorado J., Inouye M., Inouye S.:J. Bacteriol. 174, 5450–5453 (1992).PubMedGoogle Scholar

Copyright information

© Folia Microbiologica 1997

Authors and Affiliations

  • A. J. Cozzone
    • 1
  1. 1.Institut de Biologie et Chimie des ProtéinesCNRSLyonFrance

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