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Histidine phosphorylation and phosphoryl group transfer in bacterial chemotaxis

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Abstract

A cascade of protein phosphorylation, initiated by autophosphorylation of the CheA protein, may be important in the signal transduction pathway of bacterial chemotaxis. A proteolytic fragment of CheA cannot autophosphorylate, but can still transfer phosphate to proteins that generate excitation and adaptation signals. The site of CheA phosphorylation is His 48; mutants altered at this position are non-chemotactic. Similar mechanisms of transient protein phosphorylation and phosphoryl group transfer seem to be involved in processing sensory data and in activating specific gene expression.

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References

  1. Hanks, S. K., Quinn, A. M. & Hunter, T. Science 241, 42–52 (1988).

    Article  ADS  CAS  Google Scholar 

  2. Ninfa, A. J. & Magasanik, B. Proc. natn. Acad. Sci. U.S.A. 83, 5909–5913 (1986).

    Article  ADS  CAS  Google Scholar 

  3. Hess, J. F., Oosawa, K., Matsumura, P. & Simon, M. I. Proc. natn. Acad. Sci. U.S.A. 84, 7609–7613 (1987).

    Article  ADS  CAS  Google Scholar 

  4. Hess, J. F., Oosawa, K., Kaplan, N. & Simon, M. I. Cell 53, 79–87 (1988).

    Article  CAS  Google Scholar 

  5. Wylie, D., Stock, A., Wong, C.-Y. & Stock, J. Biochem. biophys. Res. Commun. 151, 891–896 (1988).

    Article  CAS  Google Scholar 

  6. Hess, J. F., Bourret, R. B., Oosawa, K., Matsumura, P. & Simon, M. I. Cold Spring Harb. Symp. quant. Biol. 53 (in the press).

  7. Clegg, D. O. & Koshland, D. E. Jr Proc. natn. Acad. Sci. U.S.A. 81, 5056–5060 (1984).

    Article  ADS  CAS  Google Scholar 

  8. Kuo, S. C. & Koshland, D. E. Jr J. Bact. 169, 1307–1314 (1987).

    Article  CAS  Google Scholar 

  9. Wolfe, A. J., Conley, P., Kramer, T. J. & Berg, H. C. J. Bact. 169, 1878–1885 (1987).

    Article  CAS  Google Scholar 

  10. Segall, J. E., Ishihara, A. & Berg, H. C. J. Bact. 161, 51–59 (1985).

    CAS  PubMed  Google Scholar 

  11. Silverman, M. & Simon, M. Nature 249, 73–74 (1974).

    Article  ADS  CAS  Google Scholar 

  12. Larsen, S. H., Reader, R. W., Kort, E. N., Tso, W-W. & Adler, J. Nature 249, 74–77 (1974).

    Article  ADS  CAS  Google Scholar 

  13. Stewart, R. C. & Dahlquist, F. W. Chem. Rev. 87, 997–1025 (1987).

    Article  CAS  Google Scholar 

  14. Parkinson, J. S. J. Bact. 135, 45–53 (1978).

    CAS  PubMed  Google Scholar 

  15. Springer, W. R. & Koshlund, D. E. Jr Proc. natn. Acad. Sci. U.S.A. 74, 533–537 (1977).

    Article  ADS  CAS  Google Scholar 

  16. Stock, J. B. & Koshland, D. E. Jr Proc. natn. Acad. Sci. U.S.A. 75, 3659–3663 (1978).

    Article  ADS  CAS  Google Scholar 

  17. Springer, M. S., Goy, M. F. & Adler, J. Nature 280, 279–284 (1979).

    Article  ADS  CAS  Google Scholar 

  18. Oosawa, K., Hess, J. F. & Simon, M. I. Cell 53, 89–96 (1988).

    Article  CAS  Google Scholar 

  19. Juhl, H. & Soderling, T. R. Math. Enzym. 99, 37–48 (1983).

    CAS  Google Scholar 

  20. Kraut, J. A. Rev. Biochem. 46, 331–358 (1977).

    Article  CAS  Google Scholar 

  21. Buss, J. E. & Stull, J. T. Meth. Enzym. 99, 7–14 (1983).

    Article  CAS  Google Scholar 

  22. Kunkel, T. A., Roberts, J. D. & Zakour, R. A. Meth. Enzym. 154, 367–382 (1987).

    Article  CAS  Google Scholar 

  23. Stader, J., Matsumura, P., Vacante, D., Dean, G. E. & Macnab, R. M. J. Bact. 166, 244–252 (1986).

    Article  CAS  Google Scholar 

  24. Wierenga, R. K. & Hol, W. G. J. Nature 302, 842–844 (1983).

    Article  ADS  CAS  Google Scholar 

  25. Kofoid, E. C. & Parkinson, J. S. Proc. natn. Acad. Sci. U.S.A. 85, 4981–4985 (1988).

    Article  ADS  CAS  Google Scholar 

  26. Burnell, J. N. & Hatch, M. D. Archs. Biochem. Biophys. 239, 175–182 (1984).

    Article  Google Scholar 

  27. Williams, S. P., Sykes, B. D. & Bridger, W. A. Biochemistry 24, 5527–5531 (1985).

    Article  CAS  Google Scholar 

  28. Pilkis, S. J., Lively, M. O. & El-Maghrabi, M. R. J. biol. Chem. 262, 12672–12675 (1987).

    CAS  PubMed  Google Scholar 

  29. Singh, B. et al. Virology 164, 114–120 (1988).

    Article  CAS  Google Scholar 

  30. Kuroda, Y. & Sharma, R. K. Biochem. biophys. Res. Commun. 112, 884–890 (1983).

    Article  CAS  Google Scholar 

  31. Deutscher, J. & Sauerwald, H. J. Bact. 166, 829–836 (1986).

    Article  CAS  Google Scholar 

  32. Robertson, E. F., Hoyt, J. C. & Reeves, H. C. J. biol. Chem. 263, 2477–2482 (1988).

    CAS  PubMed  Google Scholar 

  33. Fujitaki, J. M., Fung, G., Oh, E. Y. & Smith, R. A. Biochemistry 20, 3658–3664 (1981).

    Article  CAS  Google Scholar 

  34. Huebner, V. D. & Matthews, H. R. J. biol. Chem. 260, 16106–16113 (1985).

    CAS  PubMed  Google Scholar 

  35. Meadow, N. D., Kukuruzinska, M. A. & Roseman, S. in The Enzymes of Biological Membranes Vol. 3 (ed. Martonosi, A. N.) 523–559 (Plenum, New York, 1985).

    Book  Google Scholar 

  36. Postma, P. W. & Lengeler, J. W. Microbiol. Rev. 49, 232–269 (1985).

    CAS  PubMed  PubMed Central  Google Scholar 

  37. Adler, J. & Epstein, W. Proc. natn. Acad. Sci. U.S.A. 71, 2895–2899 (1974).

    Article  ADS  CAS  Google Scholar 

  38. Lengeler, J., Auburger, A.-M., Mayer, R. & Pecher, A. Molec. gen. Genet. 183, 163–170 (1981).

    Article  CAS  Google Scholar 

  39. Matsumura, P., Rydel, J. J., Linzmeier, R. & Vacante, D. J. Bact. 160, 36–41 (1984).

    CAS  PubMed  Google Scholar 

  40. Nixon, B. T., Ronson, C. W. & Ausubel, F. M. Proc. natn. Acad. Sci. U.S.A. 83, 7850–7854 (1986).

    Article  ADS  CAS  Google Scholar 

  41. Winans, S. C., Ebert, P. R., Stachel, S. E., Gordon, M. P. & Nester, E. W. Proc. natn. Acad. Sci. U.S.A. 83, 8278–8282 (1986).

    Article  ADS  CAS  Google Scholar 

  42. Ronson, C. W., Nixon, B. T. & Ausubel, F. M. Cell 49, 579–581 (1987).

    Article  CAS  Google Scholar 

  43. Stock, A., Chen, T., Welsh, D. & Stock, J. Proc. natn. Acad. Sci. U.S.A. 85, 1403–1407 (1988).

    Article  ADS  CAS  Google Scholar 

  44. Keener, J. & Kustu, S. Proc. natn. Acad. Sci. U.S.A. 85, 4976–4980 (1988).

    Article  ADS  CAS  Google Scholar 

  45. Weiss, V. M. & Magasanik, B. Proc. natn. Acad. Sci. U.S.A. 85 (in the press).

  46. Niederwieser, A. Meth. Enzym. 25, 60–99 (1972).

    Article  CAS  Google Scholar 

  47. Sheridan, R. C., McCullough, J. F. & Wakefield, Z. T. Inorg. Synth. 13, 23–26 (1971).

    Google Scholar 

  48. Hultquist, D. E., Moyer, R. W. & Boyer, P. D. Biochemistry 5, 322–331 (1966).

    Article  CAS  Google Scholar 

  49. Hultquist, D. E. Biochem. biophys. Acta 153, 329–340 (1968).

    CAS  PubMed  Google Scholar 

  50. Weigel, N., Kukuruzinska, M. A., Nakazawa, A., Waygood, E. B. & Roseman, S. J. biol. Chem. 257, 14477–14491 (1982).

    CAS  PubMed  Google Scholar 

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  1. Melvin I. Simon: To whom correspondence should be addressed.

Authors and Affiliations

  1. Division of Biology, California Institute of Technology, Pasadena, California, 91125, USA

    J. Fred Hess, Robert B. Bourret & Melvin I. Simon

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  1. J. Fred Hess
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  2. Robert B. Bourret
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  3. Melvin I. Simon
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Hess, J., Bourret, R. & Simon, M. Histidine phosphorylation and phosphoryl group transfer in bacterial chemotaxis. Nature 336, 139–143 (1988). https://doi.org/10.1038/336139a0

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