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Doklady Biochemistry and Biophysics

, Volume 483, Issue 1, pp 379–381 | Cite as

Calcium as a Modulator of the Adenylyl Cyclase Activity of Potato Cells in Bacterial Pathogenesis

  • N. V. Filinova
  • L. A. LomovatskayaEmail author
  • A. S. Romanenko
  • R. K. Salyaev
Biochemistry, Biophysics, and Molecular Biology
  • 6 Downloads

Abstract

This is the first study to detect the effect of calcium ions on the activity of transmembrane adenylyl cyclase (tmAC), the key enzyme of the adenylyl cyclase signaling system, under normal conditions and after a short-term exposure to exopolysaccharides (EPS) of the bacterial ring rot pathogen Clavibacter michiganensis ssp. sepedonicus (Cms). After the treatment of the roots of plants with the Cms EPS, the response to Ca2+ changed: the activity of the tmAC of plants of the resistant cultivar significantly increased, whereas in the cells of the susceptible cultivar it remained unchanged.

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References

  1. 1.
    Guo, J., Islam, A., Lin, H., Ji, C., Duan, Y., Liu, P., Zeng, Q., Day, B., and Kang, J., Front. Plant Sci., 2018, vol. 9, article 18. doi 10.3389/fpls.2018.00018Google Scholar
  2. 2.
    Hepler, P.K., Plant Cell, 2005, vol. 17, pp. 2142–2155.CrossRefGoogle Scholar
  3. 3.
    Cao, X.-Q., Juang, Z.-H., Yi, Y.-Y., Yang, Y., Ke, L.-P., Pei, Z.-M., and Zhu, S., Front Plant Sci., 2017, vol. 8, article 83.Google Scholar
  4. 4.
    Chin, K., Moeder, W., and Yoshioka, K., Botany, 2009, vol. 87, pp. 668–677.CrossRefGoogle Scholar
  5. 5.
    Halls, M.L. and Cooper, D.M.F., Cold Spring Harb. Perspect. Biol., 2011, vol. 3, p. a004143.Google Scholar
  6. 6.
    Chatukuta, P., Tshegofatso, B., Dikobe, T.B., Kawadza, D.T., Sehlabane, K.S., Mutsa, M., Takundwa, M.M., Aloysius Wong, A., Gehring, C., and Ruzvidzo, O., Biomolecules, 2018, vol. 8, no. 15. doi 10.3390/biom8020015Google Scholar
  7. 7.
    Lomovatskaya, L.A., Romanenko, A.S., and Rykun, O.V., Microbiology (Moscow), 2015, vol. 84, no. 4, pp. 473–478.CrossRefGoogle Scholar
  8. 8.
    White, P.J. and Broadley, M.R., Ann. Bot., 2003, vol. 92, pp. 487–511.CrossRefGoogle Scholar
  9. 9.
    Lomovatskaya, L.A., Romanenko, A.S., Krivolapova, N.V., Kopytchuk, V.N., and Salyaev, R.K., Dokl. Biol. Sci., 2004, vol. 394, pp. 71–73.CrossRefGoogle Scholar
  10. 10.
    Romanenko, A.S. and Lomovatskaya, L.A., Biol. Membr., 2017, vol. 34, no. 2, pp. 1–8.Google Scholar
  11. 11.
    Romanenko, A.S., Rymareva, E.V., Shafikova, T.N., and Salyaev, R.K., Dokl. Biol. Sci., 1998, vol. 358, pp. 60–62.Google Scholar
  12. 12.
    Novikova, E.M., Vodeneeva, V.A., and Sukhov, V.S., Biol. Membr., 2017, vol. 34, no. 2, pp. 109–125.Google Scholar
  13. 13.
    Shell, M.J., Thorn, P., and Irvine, R.F., J. Biol. Chem., 1998, vol. 273, no. 2, pp. 27703–27707.Google Scholar

Copyright information

© Pleiades Publishing, Inc. 2018

Authors and Affiliations

  • N. V. Filinova
    • 1
  • L. A. Lomovatskaya
    • 1
    Email author
  • A. S. Romanenko
    • 1
  • R. K. Salyaev
    • 1
  1. 1.Siberian Institute of Plant Physiology and Biochemistry, Siberian BranchRussian Academy of SciencesIrkutskRussia

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