Mikrobiol. Z. 2019; 81(4):62-75.
doi: https://doi.org/10.15407/microbiolj81.04.062

The Content of Hydrogen Peroxide and Catalase Activity in Different on Effectiveness of Symbiotic Systems
Glycine max – Bradyrhizobium japonicum under Drought Conditions

Kots S.Ya., Mamenko T.P., Homenko Yu.A.

Institute of Plant Physiology and Genetics, NAS of Ukraine
31/17 Vasylkivska Str., Kyiv, 03022, Ukraine

Aim. To investigate the effect of prolonged drought on the changes in the content of hydrogen peroxide and catalase activity in the soybean roots and root nodules by inoculation Bradyrhizobium japonicum strains and Tn-5 mutants with contrasting symbiotic properties. Methods. Microbiological, physiological, biochemical, gas chromatography, spectrophotometry. Results. It has been established that effective symbiotic systems formed with the participation of soybeans and active strains of the B. japonicum 646 and Tn-5 mutant B1-20 differed for the manifestation of catalase activity and the content of hydrogen peroxide in the roots and root nodules during the effects of drought. However, these changes were accompanied by the development of stress – protective reactions and had an adaptive nature that led to the preservation of the effective functioning of their symbiotic apparatus in conditions of drought. In symbiotic systems formed with soybean and low-active Tn-5 mutant 107 and inactive strain B. japonicum 604k, increased hydrogen peroxide content and unstable activity of the enzyme under stress, as well as a poor recovery of their level to optimal in the post-stress period, were found. Conclusions. Efficiency of functioning of symbiotic systems Glycine max – B. japonicum for prolonged exposure to drought is marked by adaptive changes in the activity of catalase in the roots and root nodules that induce the regulation of the content of hydrogen peroxide and are accompanied by the preservation the work of symbiotic apparatus.

Keywords: Glycine max (L.) Merr., Bradyrhizobium japonicum, hydrogen peroxide, catalase, reactive oxygen species, drought.

Full text (PDF, in English)

  1. Apel K, Hirt H. Reactive oxygen species: metabolism, oxidative stress, andsignal transduction. Annual Review of Plant Biology. 2004; 55:373-399. https://doi.org/10.1146/annurev.arplant.55.031903.141701
  2. Mittler R, Vanderauwera S, Gollery M, Van Breusegem F. Reactive oxygen gene network of plants. Trends in Plant Science. 2004; 9:490-498. https://doi.org/10.1016/j.tplants.2004.08.009
  3. Tognetti VB, Muhlenbock P, Van Breusegem F. Stress homeostasis - theredox and auxin perspective. Plant, Cell and Environment. 2012; 35:321-333. https://doi.org/10.1111/j.1365-3040.2011.02324.x
  4. Mittler R, Vanderauwera S, Suzuki N, et al. ROS signaling: the new wave? Trends in Plant Science. 2011; 16:300-309. https://doi.org/10.1016/j.tplants.2011.03.007
  5. Slesak I, Libik M, Karpinska B, Karpinski S, Miszalski Z. The role of hydrogen peroxide in regulation of plant metabolism and cellular signaling in response to environmental stresses. Acta Biochimica Polonica. 2007; 54:39-50.
  6. Levine A, Pennell RL., Alvarez ME., Palmer R, Lamb C. Calcium-mediated apoptosis in a plant hypersensitive disease resistance response. Current Biology. 1996; 6:427-437. https://doi.org/10.1016/S0960-9822(02)00510-9
  7. Lebrun-Garcia A, Ouaked F, Chiltz A, Pugin A. Activation of MAPK homologues by elicitors in tobacco cells. Plant J. 1998; 15:773-781. https://doi.org/10.1046/j.1365-313X.1998.00269.x
  8. Santos R, Herouart D, Puppo A, Touati D. Critical protective role of bacterial superoxide dismutase in Rhizobium-legume symbiosis. Mol. Microbiol. 2000; 38:750-759. https://doi.org/10.1046/j.1365-2958.2000.02178.x
  9. Ramu SK., Peng H-M, Cook DR. Nod factor induction of reactive oxygenspecies production is correlated with expression of the early nodulin gene rip1in Medicago truncatula. Molecular Plant-Microbe Interactions. 2002; 15:522-528. https://doi.org/10.1094/MPMI.2002.15.6.522
  10. Rubio MC, James EK, Clemente MR, et al. Localization of superoxide dismutases and hydrogen peroxide in legume root nodules. Mol. Plant Microbe Interact. 2004; 17(12):1294-1305. https://doi.org/10.1094/MPMI.2004.17.12.1294
  11. Pauly N, Pucciariello C, Mandon K, et al. Reactive oxygen and nitrogen species and glutathione: key players in the legume-Rhizobium symbiosis. Journal of Experimental Botany. 2006; 57:1769-1776. https://doi.org/10.1093/jxb/erj184
  12. Jamet A, Mandon K, Puppo A, Herouart D. H2O2 is required for optimal establishment of the Medicago sativa–Sinorhizobium meliloti symbiosis. Journal of Bacteriology. 2007; 189:8741-8745. https://doi.org/10.1128/JB.01130-07
  13. Oldroyd GE, Downie JA. Coordinating nodule morphogenesis with rhizobial infection in legumes. Annual Review of Plant Biology. 2008; 59:519-546. https://doi.org/10.1146/annurev.arplant.59.032607.092839
  14. Hérouart D, Sigaud S, Moreau S, et al. Cloning and characterization of the katA gene of Rhizobium meliloti encoding a hydrogen peroxide-inducible catalase. J. Bacteriol. 1996; 178(23):6802-6809. https://doi.org/10.1128/jb.178.23.6802-6809.1996
  15. Ohwada T, Shirakawa Y, Kusumoto M, et al. Susceptibility to hydrogen peroxide and catalase activity of root nodule bacteria. Biosci. Biotechnol. Biochem. 1999; 63(3):457-462. https://doi.org/10.1271/bbb.63.457
  16. Becana M, Dalton DA, Moran JF, et al. Reactive oxygen species and antioxidants in legume nodules. Physiol. Plant. 2000; 109:372-381. https://doi.org/10.1034/j.1399-3054.2000.100402.x
  17. Hérouart D, Baudouin E, Frendo P, et al. Reactive oxygen species, nitric oxide and glutathione: a key role in the establishment of the legume-Rhizobium symbiosis? Plant Physiol. Biochem. 2002; 40:619-624. https://doi.org/10.1016/S0981-9428(02)01415-8
  18. Matamoros MA, Dalton DA, Ramos J, et al. Biochemistry and molecular biology of antioxidants in the rhizobia - legume symbiosis. Plant Physiol. 2003; 133:499-509. https://doi.org/10.1104/pp.103.025619
  19. Glyanko AK, Akimova GP, Sokolova MG et al. [Protective and regulatory mechanisms in the development of legume-rhizobial symbiosis]. Prikladnaya biohimiya i mikrobiologiya. 2007b; 43(3):289-292. Russian.
  20. Hardy RWF, Holsten RD, Jackson EK, Burns RC. The acetylene-ethylene assay for nitrogen fixation: laboratory and field evolution. Plant Physiol. 1968; 43(8):1185-1207. https://doi.org/10.1104/pp.43.8.1185
  21. Doliba IM, Volkov RA, Panchuk II. [The method for the determination of catalase activity in roslinnogo material]. Fiziologiya i biohimiya kulturnyh rastenij. 2010; 42(6):497-503. Ukrainian.
  22. Bradford MA. Rapid and sensitive method for the quantization of the microgram quantities of protein utilizing: the principle of protein-dye binding. Anal Biochem; 1976; (72):248-254. https://doi.org/10.1006/abio.1976.9999
  23. Sagisaka S. The occurrence of peroxide in a perennial plant, Populus gelrica. Plant Physiol. 1976; 57(2):308-309. https://doi.org/10.1104/pp.57.2.308
  24. Davison PA, Hunter CN, Horton P. Overexpression of β-carotene hydroxylase enhances tolerance in Arabidopsis. Nature. 2002; 418:203-206. https://doi.org/10.1038/nature00861