|Mustakimova, E. Ch.|
|Stipanovic, Robert - Bob|
Submitted to: Meeting Proceedings
Publication Type: Proceedings
Publication Acceptance Date: 1/7/2011
Publication Date: 1/7/2011
Citation: Vshivkov, S., Akhunov, A., Golubenko, Z., Mustakimova, E., Mukhamedhanova, F., Stipanovic, R.D. 2011. Peroxidase activity in cotton cell culture infected with Verticillium dahliae. Proceedings of Beltwide Cotton Conferences, January 4-7, 2011, Atlanta, Georgia. p.55. Interpretive Summary:
Technical Abstract: In our studies with cotton, we have shown that the plant’s induced anionic peroxidases bind to chitin, which is a component of the cell wall of the plant pathogenic fungus Verticillium dahliae. In binding to the cell wall surface, they disrupt the integrity of the pathogen’s cell wall. Thus, these chitin-specific peroxidase isoforms constitute an integral part of the plant’s defense mechanism. In the present study, we investigated the response of the resistant cotton cultivar An-Baunt-2 and the susceptible cultivar C-4727 to infection with the plant pathogen Verticillium dahliae as determined by measurements of the endocellular and exocellular peroxidase activity. We found that in all samples the endocellular peroxidase was lower in comparison with extracellular isozyme activity when the tissue was challenged with V. dahliae. In a dynamic study, we found that peroxidase activity after infection with V. dahliae resulted in a sharp increase in activity, in both endocellular, and extracellular, chitin-specific peroxidases in the resistance cultivar An-Bayaut-2 within 1 hour after infection. In An-Bauut-2, maximal activity was reached in 12 hours for endocellular enzymes and 18 hours for exocellular enzymes. Enzyme activity remained at these elevated levels for 30 hours. In the case of susceptible C-4727, the response was slower and did not reach maximal levels until 18 hours after infection with V. dahliae for the extracellular enzymes and 24 hours for the endocellular enzymes; the total levels were 35 percent less than that of An-Bayaut-2.