Polymorphism of two wheat degydrines genes

  • O. Yu. Urbanovich
  • P. V. Kuzmitskaya
  • G. B. Borovskiy
DOI: https://doi.org/10.7124/FEEO.v25.1160

Abstract

Aim. The aim of this work is to study the nucleotide sequences variability of two genes encoding wheat dehydrins. One of them belong to K-2 group, the other refers to K-3 type (respectively, TaDHN18 and TaDHN19.3 according to the classification of Wang et al.). These loci sre interesting due to their's genes participation in protection of plants from the various adverse abioti ecffects. Methods. Polymorphism of two genes encoding dehydrins was investigated using 6 wheat varieties as examples, among which were spring and winter varieties with different cold resistance, using PCR-based cloning, sequencing, and data processing softwares. Results. An analysis of the obtained nucleotide and hypothetical protein sequences alignment showed that the locus under study in the genomes of different wheat varieties, both spring and winter, is characterized by a high identity degree. Conclusions. The high conservatism of two loci encoding K-2 and K-3 dehydrins was demonstrated.

Keywords: wheat, dehydrins, polymorphism.

References

Ingram J., Bartels D. The molecular basis of dehydration tolerance in plants. Annual Review of Plant Physiology and Plant Molecular Biology. 1996. Vol. 47. P. 377–403. doi: 10.1146/annurev.arplant.47.1.377.

Shinozaki K., Yamaguchi-Shinozaki K. Gene expression and signal transduction in water-stress response. Plant Physiol. 1997. Vol. 115. P. 327–334.

Shinozaki K., Yamaguchi-Shinozaki K. Molecular responses to dehydration and low temperature: Differences and cross-talk between two stress signaling pathways. Curr Opin Plant Biol. 2000. Vol. 3. P. 217–223. doi.org/10.1016/S1369-5266(00)80068-0.

Beck E.H, Heim R., Hansen J. Plant resistance to cold stress: mechanisms and environmental signals triggering frost hardening and dehardening. J Biosci. 2004. Vol. 29. P. 449–459.

Close T.J. Dehydrins: A commonalty in the response of plants to dehydration and low temperature. Physiologia Plantarum. 1997. Vol. 100. P. 291–296. doi.org/10.1111/j.1399-3054.1997.tb04785.x.

Hanin M., Brini F., Ebel C., Toda Y., Takeda S., Masmoudi K. Plant dehydrins and stress tolerance. Plant Signaling & Beha-vior. 2011. Vol. 6, I. 10. P. 1503–1509. doi: 10.4161/psb.6.10.17088.

Drira M., Saibi W., Brini F., Gargouri A., Masmoudi K., Hanin M. The K-segments of the wheat dehydrin DHN-5 are essential for the protection of lactate dehydrogenase and в-glucosidase activities in vitro. Mol Biotechnol. 2013. Vol. 54. P. 643–650. doi: 10.1007/s12033-012-9606-8.

Allagulova Ch.R, Gimalov F.R., Shakirova F.M., Vakhitov V.A. The plant dehydrins: structure and putative functions. Biochemistry. 2003. Vol. 68. P. 945–951.

Wang Y., Xu H., Zhu H., Tao Y., Zhang G., Zhang L. et al. Classification and expression diversification of wheat dehydrin genes. Plant Sci. 2014. Vol. 214. P. 113–120. doi: 10.1016/j.plantsci.2013.10.005.

Tamura K., Stecher G., Peterson D., Filipski A., Kumar S. MEGA6: Molecular Evolutionary Genetics Analysis Version 6.0. Molecular Biology and Evolution. 2013. Vol. 30. P. 2725–2729. doi: 10.1093/molbev/mst197.

Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Research. 1994. Vol. 22. P. 4673–4680.

Altschul S.F., Gish W., Miller W., Myers E.W., Lipman D.J. Basic local alignment search tool. J Mol Biol. 1990. Vol. 215. P. 403–410.