Chinese Science Bulletin

, Volume 48, Issue 5, pp 460–465 | Cite as

Protein tyrosine phosphatase is possibly involved in cellular signal transduction and the regulation of ABA accumulation in response to water deficit inMaize L. coleoptile



Water deficit-induced ABA accumulation is an ideal model or “stimulus-response” system to investigate cellular stress signaling in plant cells, using such a model the cellular stress signaling triggered by water deficit was investigated inMaize L. coleoptile. Water deficit-induced ABA accumulation was sensitively blocked by NaVO3, a potent inhibitor both to plasma membrane H+-ATPase (PM-H+-ATPase) and protein tyrosine phosphatase (PTPase). However, while PM-H+-ATPase activity was unaffected under water deficit and PM-H+-ATPase activator did not induce an ABA accumulation instead of water deficit, water deficit induced an increase in the protein phosphatase activity, and furthermore, ABA accumulation was inhibited by PAO, a specific inhibitor of PTPase. These results indicate that protein phosphtases may be involved in the cellular signaling in response to water deficit. Further studies identified at least four species of protein phosphtase as assayed by using pNPP as substrate, among which one component was especially sensitive to NaVO3. The NaVO3-sensitive enzyme was purified and finally showed a protein band about 66 kD on SDS/PAGE. The purified enzyme showed a great activity to some specific PTPase substrates at pH 6.0. In addition to NaVO3, the enzyme was also sensitive to some other PTPase inhibitors such as Zn2+ and MO3 3+, but not to Ca2+ and Mg2+, indicating that it might be a protein tyrosine phosphatase. Interestingly, the purified enzyme could be deactivated by some reducing agent DTT, which was previously proved to be an inhibitor of water deficit-induced ABA accumulation. This result further proved that PTPase might be involved in the cellular signaling of ABA accumulation in response to water deficit.


water deficit ABA H+-ATPase NaVO3 protein tyrosine phosphatase (PTPase) 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Shinozaki, K., Yamaguchi-Shinozaki, K., Gene Expression and signal transduction in water-stress response, Plant Physiol., 1997, 115: 327–334.CrossRefGoogle Scholar
  2. 2.
    Liu, Q., Zhang, Y., Chen, S., Plant protein kinase genes induced by drought, high salt and cold stresses, Chinese Science Bulletin, 2000, 45: 1153–1157.CrossRefGoogle Scholar
  3. 3.
    Neill, S. J., Burnett, E. C., Regulation of gene expression during water deficit stress, Plant Growth Regul., 1999, 29: 23–33.CrossRefGoogle Scholar
  4. 4.
    Leung, J., Giraudat, J., Abscisic acid signal transduction, Ann. Rev. Plant Physiol. Plant Mol. Biol., 1998, 49: 199–222.CrossRefGoogle Scholar
  5. 5.
    Davies, W. J., Zhang, J., Root signals and the regulation of growth and development of plants in drying soil, Ann. Rev. Plant Physiol. Plant Mol. Biol., 1991, 42: 55–76.CrossRefGoogle Scholar
  6. 6.
    Jia, W. S., He, F. L., Zhang, D. P., Cell biological mechanism for triggering of ABA accumulation under water stress inVicia faba leaves, Science In China, Ser. C, 2001, 31: 213–219.Google Scholar
  7. 7.
    Jia, W. S., Zhang, J., Water stress-induced abscisic acid accumulation in relation to reducing agents and sulhydrl modifiers in maize plant, Plant Cell Environ., 2000, 23: 1389–1395.CrossRefGoogle Scholar
  8. 8.
    Jia, W. S., Zhang, J., Initiation and regulation of water deficit-induced abscisic acid accumulation in maize leaves and roots: Cellular volume and water relations, J. Exp. Bot., 2001, 52: 295–472CrossRefGoogle Scholar
  9. 9.
    Stone, J., Dixon, J. E., Protein tyrosine phosphatases, J. Biol. Chem., 1994, 269: 3132–3133.Google Scholar
  10. 10.
    Stone, J. M., Walker, J. C., Plant protein kinase families and signal transmission, Plant Physiol., 1999, 108: 451–457.CrossRefGoogle Scholar
  11. 11.
    Guo, Y. L., Roux, S. J., Partial purification and characterization of an enzyme from pea nuclei with protein tyrosine phosphtase activity, Plant Physiol., 1995, 107: 167–173.Google Scholar
  12. 12.
    Huyer, G., Liu, S., Kelly, J. et al., Mechanism of inhibition of protein-tyrosine phosphatases by vanafate and pervanadate, J. Bio. Chem., 1997, 272: 843–851.CrossRefGoogle Scholar
  13. 13.
    Chiarugi, P., Fiaschi, T., Taddei, M. L. et al., Two vicinal cysteines confer a peculiar redox regulation to low molecular weight protein tyrosine phophatases in response to platelet-derived growth factor receptor stimulation, J. Bio. Chem., 2001, 276: 33478–33487.CrossRefGoogle Scholar
  14. 14.
    Frost, S. C., Lane, M. D., Evidence for the involvement of vicinal sulfhydrl groups in insulin-activated hexose transport by 3T3-L1 adipocytes, J. Bio. Chem., 1985, 260: 2646–2652.Google Scholar
  15. 15.
    Guo, Y. L., Terry, M. E., Roux, S. J., Characterization of a cytosolic phosphatase from pea plumules having significant protein tyrosine phosphatase activity, Plant Physiol. Biochem., 1998, 36: 269–278.CrossRefGoogle Scholar
  16. 16.
    Xu, Q., Fu, H. H., Gupta, R. et al., Molecular characterization of a tyrosine-specific protein phosphatase encoded by a stress-response gene in arabidopsis, Plant Cell, 1998, 10: 849–857.CrossRefGoogle Scholar
  17. 17.
    Tassoni, A., Antognoni, F., Bagni, N., Polyamine binding to plasma membrane vesicles isolated from zucchini hypocotyls, Plant Physiol., 1996, 110: 817–824.Google Scholar
  18. 18.
    Chen, P. S., Toribara, T. Y., Warner, H., Microdetermination of phosphorus, Analytical Chem. 1956, 28: 1756–1758.CrossRefGoogle Scholar
  19. 19.
    Quarrie, S. A., Whitford, P. N., Appleford, N. E. J. et al., A monoclonal antibody to (S)-abscisic acid: Its characterization and use in a radio immunoassay for measuring abscisic acid in crude extracts of cereal and lupin leaves, Planta, 1988, 173: 330–339.CrossRefGoogle Scholar
  20. 20.
    Ng, D. H. W., Harder, K. W., Clark-Lewis, I. et al., Nonradioactive method to measure CD45 protein tyrosine phosphatase activity isolated directly from cells, J. Immunol. Methods, 1994, 179: 177–185.CrossRefGoogle Scholar
  21. 21.
    Sheen, J., Ca2+-dependent protein kinases and stress signal transduction in plants, Science, 1996, 274: 1900–1902.CrossRefGoogle Scholar
  22. 22.
    Stone, J. M., Walker, J. C., Plant protein kinase families and signal transmission, Plant Physiol., 1995, 108: 451–457.CrossRefGoogle Scholar
  23. 23.
    Chang, C., Stewart, R. C., The two-component system, Plant Physiol., 1998, 117: 723–731.CrossRefGoogle Scholar
  24. 24.
    Urao, T., Yakubov, B., Satoh, R. et al., A transmembrane hybrid-type histidine kinase in arabidopsis function as an osmosensor, Plant Cell, 1999, 11: 1743–1754.CrossRefGoogle Scholar

Copyright information

© Science in China Press 2003

Authors and Affiliations

  • Yu Xing
    • 2
  • Shuqiu Zhang
    • 1
  • Youqun Wang
    • 1
  • Wensuo Jia
    • 1
    • 2
  1. 1.National Key Laboratory of Plant Physiology and BiochemistryChina Agricultural UniversityBeijingChina
  2. 2.School of Agronomy and BiotechnologyChina Agricultural UniversityBeijingChina

Personalised recommendations