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Molecular peculiarities of the chitin-binding peroxidases of plants

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Abstract

The chitin-binding ability of isoperoxidases isolated from 23 plants of different species was studied. The activation of peroxidases in a protein extract in the presence of this polysaccharide was found for 14 of the studied plants. Anionic isoperoxidases were shown to be sorbed on chitin and eluted from them with 1M NaCl for 16 of the plant species. Cationic isoforms of the peroxidases of some species of the Fabaceae and Cucurbitaceae plant families also bound to chitin. An immunochemical similarity was found between the chitin-binding isoperoxidases of taxonomically distant plant species (the Pomaceous, Fabaceae, and Cucurbitaceae). Moreover, a high homology of the molecular structures of the polysaccharide-binding sites was revealed for the anionic peroxidases of rice, wheat, oat, zucchini, cucumber, and radish. We propose the existence of a special class of plant peroxidases that bind with polysaccharides (chitin) and participate in the protective reactions of plants against pathogens.

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References

  1. Lagrimini, M.L., Gingas, V., Finger, T., Rothstein, S., and Liu, T., Plant Physiol., 1997, vol. 114, pp. 1187–1196.

    CAS  PubMed  Google Scholar 

  2. Ito, H., Hiraga, S., Tsugawa, H., Matsui, H., Honma, M., Otsuki, Y., Murakami, T., and Ohashi, Y., Plant Sci., 2000, vol. 155, pp. 85–100.

    Article  CAS  PubMed  Google Scholar 

  3. Welinder, K.G., Justesen, A.F., Kjarsgåd, I.V., Jensen, R.B., Rasmussen, S.K., Jespersen, H.M., and Duroux, L., Eur. J. Biochem., 2002, vol. 269, pp. 6063–6081.

    Article  CAS  PubMed  Google Scholar 

  4. Duroux, L. and Welinder, K.L., J. Mol. Evol., 2003, vol. 57, pp. 397–407.

    Article  CAS  PubMed  Google Scholar 

  5. Cairns, E., van Huystee, R.B., and Cairns, W.L., Physiol. Plant., 1979, vol. 49, pp. 78–82.

    Article  Google Scholar 

  6. Conroy, J.M., Borzelleca, D.C., and McDonell, L.A., Plant Physiol., 1982, vol. 69, pp. 28–31.

    Article  CAS  PubMed  Google Scholar 

  7. Khairullin, R.M., Yusupova, Z.R., and Maksimov, I.V., Fiziol. Rast., 2000, vol. 47, pp. 108–113.

    Google Scholar 

  8. Maksimov, I.V., Cherepanova, E.A., Yarullina, L.G., and Akhmetova, I.E., Prikl. Biokhim. Mikrobiol., 2005, vol. 41, pp. 616–620.

    CAS  PubMed  Google Scholar 

  9. Burkhanova, G.F., Yarullina, L.G., and Maksimov, I.V., Fiziol. Rast., 2007, vol. 54, pp. 119–126.

    Google Scholar 

  10. http://peroxidase.isb-sib.ch/

  11. http://ncbi.nlm.nih.gov

  12. Rebmann, G., Hertig, C., Bull, J., Mauch, F., and Dudler, R., Plant. Mol. Biol., 1991, vol. 16, pp. 329–331.

    Article  CAS  PubMed  Google Scholar 

  13. Cheng, E.H., Kirsch, D.G., Clem, R.J., Ravi, R., Kastan, M.B., Bedi, A., Ueno, K., and Hardwick, J.M., Science, 1997, vol. 278, pp. 1966–1968.

    Article  CAS  PubMed  Google Scholar 

  14. Riemann, C., Ringli, C., and Dudler, R., Plant Physiol., 1992, vol. 100, pp. 1611–1612.

    Article  Google Scholar 

  15. Chittoor, J.M., Leach, J.E., and White, F.F., Mol. Plant-Microbe Inter., 1997, vol. 10, pp. 861–871.

    Article  CAS  Google Scholar 

  16. Padegimas, L.S. and Reichert, N.A., Nematode-Upregulated Peroxidase Gene Promoter from Nematode-Resistant Maize Line Mp307, US Patent No. 6703541, 2004.

  17. Guillet-Claude, C., Birolleau-Touchard, C., Manicacci, D., Rogowsky, P.M., Rigau, J., Murigneux, A., Martinant, J.P., and Barriere, Y., BMC Genet., 2004, vol. 5, p. 19.

    Article  PubMed  Google Scholar 

  18. Teichmann, T., Guan, C., Kristoffersen, P., Muster, G., Tietz, O., and Palme, K., Eur. J. Biochem., 1997, vol. 247, pp. 826–832.

    Article  CAS  PubMed  Google Scholar 

  19. Fujiyama, K., Takemura, H., Shinmyo, A., Okada, H., and Takano, M., Gene, 1990, vol. 89, pp. 163–169.

    Article  CAS  PubMed  Google Scholar 

  20. Dunand, C., Tognolli, M., Overney, S., von Tobel, L., Meyer, M., Simon, P., and Penel, C., J. Plant Physiol., 2002, vol. 159, pp. 1165–1171.

    Article  CAS  Google Scholar 

  21. Shibuya, N. and Minami, E., Physiol. Mol. Plant Pathol., 2001, vol. 59, pp. 223–233.

    Article  CAS  Google Scholar 

  22. Roberts, E., Kutchan, T., and Kolattukudy, P.E., Plant. Mol. Biol., 1988, vol. 11, pp. 15–26.

    Article  CAS  Google Scholar 

  23. Diaz-De-Leon, F., Klotz, K.L., and Lagrimini, L.M., Plant Physiol., 1993, vol. 101, pp. 1117–1118.

    Article  CAS  PubMed  Google Scholar 

  24. Carpin, S., Crevecoeur, M., Greppin, H., and Penel, C., Plant Physiol., 1999, vol. 120, pp. 799–810.

    Article  CAS  PubMed  Google Scholar 

  25. Yan, J., Wang, J., Tissue, D., Holaday, A.S., Allen, R., and Zhang, H., Crop Sci., 2003, vol. 43, pp. 1477–1483.

    Article  CAS  Google Scholar 

  26. Shul’gin, K.K., Popova, T.N., and Rakhmanova, T.I., Prikl. Biokhim. Mikrobiol., 2008, vol. 44, pp. 276–280.

    Google Scholar 

  27. Ozeretskovskaya, O.L., Vasyukova, N.I., and Zinov’eva, S.V., Khitin i khitozan: Poluchenie, svoistva i primenenie (Chitin and Chitosan: Obtaining, Properties, and Application), Skryabin, K.G., Vikhoreva, G.A., and Varlamov, V.P., Eds., Moscow: Nauka, 2002, pp. 339–345.

    Google Scholar 

  28. Ermakov, A.I., Methody biokhimicheskogo issledovaniya rastenii (Methods in Plant Biochemistry), Leningrad: Agropromizdat, 1987.

    Google Scholar 

  29. Beilez, E.M., Richardson, P.J, and Luzio, J.P., Biologicheskie membrany. Metody (Biological Membranes: Methods), Findlei, J.B. and Evans, U.G., Eds., Moscow: Mir, 1990.

    Google Scholar 

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Authors and Affiliations

  1. Institute of Biochemistry and Genetics, Ufa Scientific Center, Russian Academy of Sciences, pr. Oktyabrya 71, Ufa, 450054, Russia

    I. V. Maksimov, E. A. Cherepanova, O. I. Kuzmina & L. G. Yarullina

  2. Sadykov Institute of Bioorganic Chemistry, Academy of Sciences of the Republic Of Uzbekistan, Tashkent, 700125, Uzbekistan

    A. A. Akhunov

Authors
  1. I. V. Maksimov
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  2. E. A. Cherepanova
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  3. O. I. Kuzmina
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  4. L. G. Yarullina
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  5. A. A. Akhunov
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Correspondence to I. V. Maksimov.

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Original Russian Text © I.V. Maksimov, E.A. Cherepanova, O.I. Kuzmina, L.G. Yarullina, A.A. Akhunov, 2010, published in Bioorganicheskaya Khimiya, 2010, Vol. 36, No. 3, pp. 319–326.

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Maksimov, I.V., Cherepanova, E.A., Kuzmina, O.I. et al. Molecular peculiarities of the chitin-binding peroxidases of plants. Russ J Bioorg Chem 36, 293–300 (2010). https://doi.org/10.1134/S1068162010030039

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  • DOI: https://doi.org/10.1134/S1068162010030039

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