Year: 2022
Pages: 238-242
Number: Volume 14, issue 3
Type: scientific article
DOI: https://doi.org/10.31301/2221-6197.bmcs.2022-19
Topic: Article
Authors: Tugbaeva A.S., Ermoshin A.A., Kiseleva I.S.
The effect of copper ions (100 and 200 μM CuSO4) in a long-term experiment on the activity of class III peroxidases and PRX gene expression level in the root and stem of juvenile zinnia plants was studied. It was found that an increase in the content of copper ions in the root system was accompanied by the rise of hydrogen peroxide, which led to the growth of the activity of neutral guaiacol peroxidase (GPO) and acid benzidine peroxidase (BPO). The relative number of PRX gene transcripts also increased in the root that caused additional lignification, especially, Klason lignin. In the stem, the copper content in the experimental plants was comparable to the control level. An increase in the activity of peroxidases contributed to a decrease in the amount of hydrogen peroxide in this organ and was accompanied by a compensatory rise in the lignin content. The increase of the expression level of PRX gene suggests its role in the formation of plant resistance to the prolonged impact of copper ions due to enhanced lignification of cell walls.
cell walls, lignification, metaxylem, class III peroxidases, phenols, heavy metals
1. Barcelo A.R., Gomez Ros L.V., Gabaldon C., Lopez-Serrano M., Pomar F., Carrion J.S., Pedreño M.A. Basic peroxidases: the gateway for lignin evolution? Phytochem. Rev. 2004. V.3. P.61‒78. doi: 10.1023/B:PHYT.0000047803.49815.1a
2. Bellincampi D., Dipierro N., Salvi G., Cervone F., De Lorenzo G. Extracellular H2O2 induced by oligogalacturonics is not involved in the inhibition of the auxin-regulated rolB gene expression in tobacco leaf explants. Plant Physiol. 2000. V. 122. P. 1379–1385. doi: 10.1104/pp.122.4.1379
3. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976. V. 72. P. 248–254. doi: 10.1006/abio.1976.9999
4. Carrier M., Loppinet Serani A., Denux D., Lasnier J., Ham Pichavant F., Cansell F., Aymonier C. Thermogravimetric analysis as a new method to determine the lignocellulosic composition of biomass. Biomass Bioenergy. 2011. V. 35. P. 298–307. doi: 10.1016/j.biombioe.2010.08.067
5. Chance B. Maehly A.C. Assay catalase and peroxidase // Methods Enzymol. 1955. V. 2. P. 764–775. doi:10.1002/9780470110171.CH14
6. Elleuch A., Chaâbene Z., Grubb D.C., Drira N., Mejdoub H., Khemakhem B. Morphological and biochemical behavior of fenugreek (Trigonella foenumgraecum) under copper stress. Ecotoxicol. Environ. Saf. 2013. V. 98. P. 46–53. doi: 10.1016/j.ecoenv.2013.09.028
7. GoldfischerS., Essner R. Further observation of the peroxidase activities of microbodies (peroxisomes). J. Histochem. Cytochem. 1969. V. 17. P. 681–685. doi: 10.1177/17.10.681
8. Gómez-Ros L.V., Gabaldón C., Núñez-Flores M.J.L., Gutiérrez J., Herrero J., Zapata J.M., Sottomayor M., Juan Cuello J., Barceló A.R. The promoter region of the Zinnia elegans basic peroxidase isoenzyme gene contains cis-elements responsive to nitric oxide and hydrogen peroxide. Planta. 2012. V. 236. P. 327–342. doi: 10.1007/s00425-012-1604-3
9. Jovanovic S.V., KukavicaB., Vidovic M., Morina F., Menckhoff L. Class III peroxidases: Functions, localization and redox regulation of isoenzymes. Antioxid. Antioxid. Enzym. High. Plants. 2018. P. 269–300. doi: 10.1007/978-3-319-75088-0_13
10. Liu Q., Luo L., Zheng L. Lignins: biosynthesis and biological functions in plants. Int. J. Mol. Sci. 2018. V. 19(2). P. 335. doi: 10.3390/ijms 19020335
11. Passardi F., Longet D., Penel C., Dunand C. The class III peroxidase multigenic family in rice and its evolution in land plants. Phytochem. 2004. V. 65. P. 1879–1893. doi: 10.1016/j.phytochem.2004.06.023
12. Sato Y., Demura T., Yamawaki K., Inoue Y., Sato S., Sugiyama M., Fukuda H. Isolation and characterization of a novel peroxidase gene ZPO-C whose expression and function are closely associated with lignification during tracheary element differentiation. Plant Cell Physiol. 2006. V. 4(47). P. 493‒503. doi: 10.1093/pcp/pcj016
13. Tugbaeva A., Ermoshin A., Plotnikov D., Wuriyanghan H., Kiseleva I. Role of class III peroxidases in stem lignification of Zinnia elegans Jacq. Biol. Life Sci. Forum. 2021. V. 4. P. 22. doi: 10.3390/IECPS2020-08847
14. Tugbaeva A., Ermoshin A., Wuriyanghan H., Maleva M., Borisova G., Kiseleva I. Copper stress enhances the lignification of axial organs in Zinnia elegans. Horticulturae. 2022. V. 8. P. 558. doi: 10.3390/horticulturae8060558
15. Yasuda S., Fukushima K., Kakehi A. Formation and chemical structures of acid-soluble lignin I: Sulfuric acid treatment time and acid-soluble lignin content of hardwood. J. Wood Sci. 2001. V. 47. P. 69–72. doi: 10.1007/BF00776648