Ascorbate peroxidase of moss Dicranum scoparium: gene identification, enzyme activity
- Authors: Onele A.O.1, Chasov A.V.1,2, Trifonova T.V.1, Minibayeva F.V.1,2
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Affiliations:
- Kazan Institute of Biochemistry and Biophysics, FRC Kazan Scientific Center of the Russian Academy of Sciences
- Kazan Federal University
- Issue: Vol 489, No 4 (2019)
- Pages: 424-428
- Section: Biochemistry, biophysics, molecular biology
- URL: https://journals.eco-vector.com/0869-5652/article/view/18702
- DOI: https://doi.org/10.31857/S0869-56524894424-428
- ID: 18702
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Abstract
In present work, the APX gene encoding ascorbate peroxidase in the moss Dicranum scoparium was for the first time cloned and sequenced, high homology of APX with ascorbate peroxidase genes of the mosses Grimmia pilifera and Physcomitrella patens was shown. The structure of the protein was characterized using bioinfomatics approach and the activity of the enzyme under abiotic stresses was studied. An increase in the activity of ascorbate peroxidase was detected during desiccation of D. scoparium shoots. When exposed to heat shock, a decrease in the acti-vity of ascorbate peroxidase correlated with a decrease in the expression of APX. Conserved elements, which were found in the structure of ascorbate peroxidase gene and protein, indicate that these sequences are preserved in the plant genome during evolution, in support of the importance of this enzyme in maintaining cellular redox status.
About the authors
A. O. Onele
Kazan Institute of Biochemistry and Biophysics, FRC Kazan Scientific Center of the Russian Academy of Sciences
Email: minibayeva@kibb.knc.ru
Russian Federation, 2/31, Lobachevsky street, Kazan, Republic of Tatarstan, 420111
A. V. Chasov
Kazan Institute of Biochemistry and Biophysics, FRC Kazan Scientific Center of the Russian Academy of Sciences; Kazan Federal University
Email: minibayeva@kibb.knc.ru
Russian Federation, 2/31, Lobachevsky street, Kazan, Republic of Tatarstan, 420111; 18, Kremliovskaya street, Kazan, 420008
T. V. Trifonova
Kazan Institute of Biochemistry and Biophysics, FRC Kazan Scientific Center of the Russian Academy of Sciences
Email: minibayeva@kibb.knc.ru
Russian Federation, 2/31, Lobachevsky street, Kazan, Republic of Tatarstan, 420111
F. V. Minibayeva
Kazan Institute of Biochemistry and Biophysics, FRC Kazan Scientific Center of the Russian Academy of Sciences; Kazan Federal University
Author for correspondence.
Email: minibayeva@kibb.knc.ru
Russian Federation, 2/31, Lobachevsky street, Kazan, Republic of Tatarstan, 420111; 18, Kremliovskaya street, Kazan, 420008
References
- Foyer C.H. // Environ. Exp. Bot. 2018. V. 154. P. 134-142. https://doi.org/10.1016/j.envexpbot.2018.05.003
- Gest N., Gautier H., Stevens R. // J. Exp. Bot. 2013. V. 64. P. 33-53. https://doi.org/10.1093/jxb/ers297
- Smirnoff N. // Free Radic. Biol. Med. 2018. V. 122. P. 116-129. https://doi.org/10.1016/j.freeradbiomed.2018.03.033
- Onele A.O., Chasov A., Viktorova L., et al. // S. Afr. J. Bot. 2018. V. 119. P. 132-141. https://doi.org/10.1016/j.sajb.2018.08.014
- Li X., Zhang D., Li H., et al. // Front. Plant Sci. 2015. V. 6. P. 38. https://doi.org/10.3389/fpls.2015.00038
- Song X.H., Sha W., Jin Z.M., et al. // Adv. Intel. Soft. Compu. 2012. V. 134. P. 433-440. https://doi.org/10.1007/978-3-642-27537-1_53
- Rushmore T.H., Morton M.R., Pickett C.B.J. // Biol. Chem. 1991. V. 266. P. 11 632-11 639.
- Dabrowska G., Kata A., Goc A., et al. // Acta Biol. Crac. 2007. V. 1. P. 7-17.
- Jespersen H.M., Kjaersgard I.V.H., Ostergaard L., et al. // Biochem. J. 1997. V. 326. P. 305-310. https://doi.org/10.1042/bj3260305
- Celik A., Cullis P.M., Sutcliffe M.J., et al. // Eur. J. Biochem. 2001. V. 268. P. 78-85. https://doi.org/10.1046/j.1432-1327.2001.01851.x
- Bursey E.H., Poulos T.L. // Biochemistry. 2000. V. 39. P. 7374-737. https://doi.org/10.1021/ bi000446s
- Lubaina A.S., Meenu Krishnan V.G., Murugan K. // Indian J. Plant Sci. 2013. V. 2. P. 12-22.