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Nucleoside Diphosphate Kinase Is a Possible Component of the Ethylene Signal Transduction Pathway

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Abstract

In etiolated seedlings of Pisum sativum and leaves of Arabidopsis thaliana, in vivo ethylene treatment resulted in an increase in in vitro phosphorylation of 17 kD (P. sativum) or 16 and 17 kD (A. thaliana) polypeptides. These polypeptides were identified as nucleoside diphosphate kinase (NDPK) based on both biochemical properties and interaction with antibodies against NDPK from P. sativum. Using the receptor-directed antagonist of ethylene action 2,5-norbornadiene and the ethylene-insensitive mutants of A. thaliana etr1-1 and eti5, ethylene specificity and receptor dependence of NDPK phosphorylation have been demonstrated. In pea epicotyls, ethylene treatment also led to increase in nucleoside transferase activity unlike in A. thaliana leaves. The increases in nucleoside transferase activity and NDPK phosphorylation were very rapid and transient. The results suggest a role for NDPK as a possible component of the ethylene signal transduction chain.

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REFERENCES

  1. Parks, R. E., Jr., and Agarwal, R. P. (1973) in The Enzymes (Boyer, P. D., ed.) Vol. 8, Academic Press, New York, pp. 307-333.

    Google Scholar 

  2. Dumas, C., Lascu, I., Morera, S., Glaser, P., Fourme, R., Wallet, V., Veron, M., and Janin, J. (1992) EMBO J., 11, 3203-3208.

    Google Scholar 

  3. Munoz-Dorado, J., Inouye, S., and Inouye, M. (1990) J. Biol. Chem., 265, 2707-2712.

    Google Scholar 

  4. Postel, E. H., Berberich, S. J., Flint, S. J., and Ferrone, C. A. (1993) Science, 261, 478-480.

    Google Scholar 

  5. Moisyadi, S., Dharmasiri, S., Harrington, H. M., and Lukas, T. J. (1994) Plant Physiol., 104, 1401-1409.

    Google Scholar 

  6. MacDonald, N. J., De La Rosa, A., Benedict, M. A., Freije, J. M. P., Krutsch, H., and Steeg, P. S. (1993) J. Biol. Chem., 268, 25780-25789.

    Google Scholar 

  7. Bovet, L., and Siegenthaler, P._A. (1997) Plant Physiol. Biochem., 35, 455-465.

    Google Scholar 

  8. Cipollini, G., Berti, A., Fiore, L., Rainaldi, G., Basolo, F., Merlo, G., Bevilacqua, G., and Caligo, M. (1997) Int. J. Cancer, 73, 297-302.

    Google Scholar 

  9. Ji, L., Arcinas, M., and Boxer, L. M. (1995) J. Biol. Chem., 270, 13392-13398.

    Google Scholar 

  10. Engel, M., Seifert, M., Theisinger, B., Seyfert, U., and Welter, C. (1998) J. Biol. Chem., 273, 20058-20065.

    Google Scholar 

  11. Wagner, P. D., and Vu, N.-D. (2000) Biochem. J., 346, 623-630.

    Google Scholar 

  12. Zimmermann, S., Baumann, A., Jaekel, K., Marback, I., Engelberg, D., and Frohnmeyer, H. (1999) J. Biol. Chem., 274, 17017-17024.

    Google Scholar 

  13. Choi, G., Yi, H., Lee, J., Kwon, Y. K., Soh, M. S., Shin, B., Luka, Z., Hahr, T. R., and Song, P. S. (1999) Nature, 401, 610-613.

    Google Scholar 

  14. Harris, N., Taylor, J. E., and Roberts, J. A. (1994) Plant Mol. Biol., 25, 739-742.

    Google Scholar 

  15. Galvis, M. L. E., Marttila, S., Hakansson, G., Forsberg, J., and Knorpp, C. (2001) Plant Physiol., 126, 69-77.

    Google Scholar 

  16. Novikova, G. V., Moshkov, I. E., Smith, A. R., Kulaeva, O. N., and Hall, M. A. (1999) Planta, 208, 239-246.

    Google Scholar 

  17. Sisler, E. C., Blankenship, S. M., and Guest, M. (1990) Plant Growth Regul., 9, 157-164.

    Google Scholar 

  18. Struglics, A., and Hakansson, G. (1999) Eur. J. Biochem., 262, 765-773.

    Google Scholar 

  19. Schaertl, S., Konrad, M., and Geeves, M. A. (1998) J. Biol. Chem., 273, 5662-5669.

    Google Scholar 

  20. Ann, K.-S., and Nelson, D. L. (1996) J. Eucaryot. Microbiol., 43, 365-372.

    Google Scholar 

  21. Bleecker, A. B., Estelle, M. A., Somerville, C., and Kende, H. (1988) Science, 241, 1086-1089.

    Google Scholar 

  22. Sanders, I. O., Harpham, N. V. J., Raskin, I., Smith, A. R., and Hall, M. A. (1991) Ann. Bot., 68, 97-103.

    Google Scholar 

  23. Lu, Q., Park, H., Egger, L. A., and Inouye, M. (1996) J. Biol. Chem., 271, 32886-32893.

    Google Scholar 

  24. Yano, A., Umeda, M., and Uchimiya, H. (1995) Plant Mol. Biol., 27, 1053-1058.

    Google Scholar 

  25. Pan, L., Kawai, M., Yano, A., and Uchimiya, H. (2000) Plant Physiol., 122, 447-452.

    Google Scholar 

  26. Biggs, J., Hersperger, E., Steeg, P. S., Liotta, L. A., and Shearn, A. (1990) Cell, 63, 922-940.

    Google Scholar 

  27. Lombardi, D., Sacchi, A., D'Agostino, G., and Tibursi, G. (1995) Exp. Cell Res., 217, 267-271.

    Google Scholar 

  28. Shibaoka, H. (1991) in The Cytoskeletal Basis of Plant Growth and Form (Lloyd, C. W., ed.) Academic Press, New York, pp. 159-168.

    Google Scholar 

  29. Bominaar, A. A., Molijn, A. C., Pestel, M., Veron, M., and van Haastert, P. J. M. (1993) EMBO J., 12, 2275-2279.

    Google Scholar 

  30. Lagnado, L., and Baylor, D. (1992) Neuron, 8, 995-1002.

    Google Scholar 

  31. Klinker, J. F., Hageluken, A., Grunbaum, L., Heilmann, I., Nurnberg, B., Harhammer, R., Offermann, S., Schwaner, I., Ervens, J., Wenzelseifert, K., Muller, T., and Seifert, R. (1994) Biochem J., 304, 377-383.

    Google Scholar 

  32. Chopade, B. A., Shankar, S., Sundin, G. W., Mukhopadhyay, S., and Chakrabarty, A. M. (1997) J. Bacteriol., 179, 2181-2188.

    Google Scholar 

  33. Moshkov, I. E., Novikova, G. V., Mur, L. A. J., Smith, A. R., and Hall, M. A. (2003) Plant Physiol., 131, 1718-1726.

    Google Scholar 

  34. Hall, A. (ed.) (2000) GTPases, Oxford University Press, Oxford.

    Google Scholar 

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Novikova, G.V., Moshkov, I.E., Smith, A.R. et al. Nucleoside Diphosphate Kinase Is a Possible Component of the Ethylene Signal Transduction Pathway. Biochemistry (Moscow) 68, 1342–1348 (2003). https://doi.org/10.1023/B:BIRY.0000011656.90378.e4

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  • DOI: https://doi.org/10.1023/B:BIRY.0000011656.90378.e4

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