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Expression analysis and molecular modelling of hydrophilin LEA-2-like gene from wheat

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Abstract

The inquisitive role of boiling soluble proteins is still not well documented. Hence, this study demonstrated isolation, and sequencing of a water stress responsive cDNA which encodes LEA-like boiling soluble proteins (designated as TaBsSRP3 Triticum aestivum boiling soluble stress responsive proteins) from waters stressed seedlings from wheat (PBW 175) cultivar tolerant to drought stress. qRT-PCR analysis revealed high drought stress induced expression of TaBsSRP3 in tolerant cv. PBW 175. However, the level of TaBsSRP3 was substantially less in the susceptible cv. PBW 343. We described in-silico analysis and 3D modelling of TaBsSRP3 which predicted it as stress-responsive and boiling stable stable protein. The physio-chemical analysis of TaBsSRP3 revealed that it belongs to group 2 LEA proteins. Based upon these findings, it was postulated that how these boiling soluble proteins preclude the unfavourable effects of water stress.

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References

  • Battaglia, M., Olvera-CarrilloY, G. A., Campos, F., & Covarrubias, A. A. (2008). The enigmatic LEA proteins and other hydrophilins. Plant Physiology, 148, 6–24.

    Article  CAS  Google Scholar 

  • Bravo, L. A., Gallardoa, J., Navarretea, A., et al. (2003). Cryoprotective activity of a cold induced dehydrin purified from barley. Physiologia Plantarum, 118, 262–269.

    Article  CAS  Google Scholar 

  • Bravo, L. A., Gallardoa, J., Navarretea, A., et al. (2003b). Cryoprotective activity of a cold induced dehydrin purified from barley. Physiologia Plantarum, 118, 262–269.

    Article  CAS  Google Scholar 

  • Brini, F., Saibi, W., Amara, I., Gargouri, A., Masmoudi, K., & Hanin, M. (2010). Wheat dehydrin DHN-5 exerts a heat protective effect on β- Glucosidase and glucose oxidase activities. Bioscience Biotechnology and Biochemistry, 74, 1050–1054.

    Article  CAS  Google Scholar 

  • Danyluk, J., Perron, A., Houde, M., et al. (1998). Accumulation of an acidic dehydrin in the vicinity of the plasma membrane during cold acclimation of wheat. The Plant Cell, 10, 623–638.

    Article  CAS  Google Scholar 

  • Fox, S. J., & Kannan, S. (2017). Probing the dynamics of disorder. Progress in Biophy Molecular Biology, 128, 57–62.

    Article  CAS  Google Scholar 

  • Garay- Arroyo, A., Flores, J. M. C., & Garciarrubio, A. C. (2000). Highly hydrophilic proteins in prokaryotes and eukaryotes are common during conditions of water deficit. Journal of Biological Chemistry, 275, 5666–5674.

    Article  Google Scholar 

  • Goyal, K., Walton, L. J., & Tunnacliffe, A. (2005). LEA proteins prevent protein aggregation due to water stress. The Biochemical Journal, 388, 151–157.

    Article  CAS  Google Scholar 

  • Graether, S. P., & Boddington, K. F. (2014). Disorder and function: A review of the dehydrin protein family. Frontiers in Plant Science, 5, 1–12.

    Article  Google Scholar 

  • Grelet, J., Benamer, A., Teyssier, E., Avelange-Macherel, M. H., Grunwald, D., & Macherel, D. (2005). Identification in pea seed mitochondria of a late embryogenesis abundant protein able to protect enzymes from drying. Plant Physiology, 137, 157–167.

    Article  CAS  Google Scholar 

  • Hanin, M., Brini, F., Ebel, C., Toda, Y., Takeda, S., & Masmoudi, K. (2011). Plant dehydrins and stress tolerance: Versatile proteins for complex mechanisms. Plant Signaling and Behavior, 6, 1503–1509.

    Article  CAS  Google Scholar 

  • Hara, M., Shinoda, Y., Tanaka, Y., & Kuboi, T. (2009). DNA binding of citrus dehydrin promoted by zinc ion. Plant Cell and Environment, 32, 532–541.

    Article  CAS  Google Scholar 

  • Hughes, S., & Graether, S. P. (2011). Cryoprotective mechanism of a small intrinsically disordered dehydrin protein. Protein Science, 20, 42–50.

    Article  CAS  Google Scholar 

  • Koag, M. C., Fenton, R. D., & WilkensS, C. T. J. (2003). The binding of maize DHN1 to lipid vesicles. Gain of structure and lipid specificity. Plant Physiology, 131, 309–316.

    Article  CAS  Google Scholar 

  • Kovacs, D., Kalmar, E., Torok, Z., & Tompa, P. (2008). Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins. Plant Physiology, 147, 381–390.

    Article  CAS  Google Scholar 

  • Mouillon, J. M., Gustafsson, P., & Harryson, P. (2006). Structural investigation of disordered stress proteins: Comparison of full-length dehydrins with isolated peptides of their conserved segments. Plant Physiology, 141, 638–650.

    Article  CAS  Google Scholar 

  • Rakhra, G., Kaur, T., Vyas, D., & Sharma, A. D. (2017). Molecular cloning, characterization, heterologous expression and in- silico analysis of disordered boiling soluble stress-responsive wBsSRP protein from drought tolerant wheat cv.PBW 175. Plant Physiology and Biochemistry, 112, 29–44.

    Article  CAS  Google Scholar 

  • Rorat, T. (2006). Plant dehydrins-tissue location, structure and function. Cellular and Molecular Biology Letters, 11, 536–556.

    Article  CAS  Google Scholar 

  • Saibi, W., Feki, K., Mahmoud, R. B., & Brini, F. (2015). Durum wheat dehydrin (DHN-5) confers salinity tolerance to transgenic arabidopsis plants through the regulation of proline metabolism and ROS scavenging system. Planta, 242, 1187–1194.

    Article  CAS  Google Scholar 

  • Tsvetanov, S., Ohno, R., Tsuda, K., et al. (2000). A cold-responsive wheat (Triticum aestivum L.) gene wcor14 identified in a winter-hardy cultivar ’Mironovska 808’. Genes and Genetic Systems, 75, 49–57.

    Article  CAS  Google Scholar 

  • Uversky, V. N. (2002). What does it mean to be natively unfolded? European Journal of Biochemistry, 269, 2–12.

    Article  CAS  Google Scholar 

  • Yang, Y., Sun, X., YangS, L. X., & Yang, Y. (2014). Molecular cloning and characterization of a novel SK3-type dehydrin gene from Stipapurpurea. Biochemical and Biophysical Research Communications, 448, 145–150.

    Article  CAS  Google Scholar 

  • Yoshida, T., Fujita, Y., Sayama, H., et al. (2010). AREB1, AREB2, and ABF3 are master transcription factors that cooperatively regulate ABRE-dependent ABA signaling involved in drought stress tolerance and require ABA for full activation. The Plant Journal, 61, 672–685.

    Article  CAS  Google Scholar 

  • Zhu, W., Zhang, L., Zhang, N., Xing, Y., & Jiang, B. (2012). The clone of wheat dehydrin-like gene wzy2 and its functional analysis in Pichiapastoris. African Journal of Biotechnology, 11, 9549–9558.

    CAS  Google Scholar 

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Funding

Financial assistance for this work was provided by the UGC (University Grants Commission), New Delhi (India) in form of major research project.

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Author notes

  1. Gurmeen Rakhra

    Present address: Department of Biochemistry, School of Bioengineering and Biosciences, Lovely Professional University, Delhi G.T. Road, - Phagwara, Jalandhar, Punjab, 144411, India

Authors and Affiliations

  1. PG Department of Biotechnology, Lyallpur Khalsa College, G.T. Road, Jalandhar, Punjab, 144001, India

    Arun Dev Sharma & Gurmeen Rakhra

  2. Biodiversity and Applied Botany Division Indian Institute of Integrative Medicine (CSIR) Canal Road, Jammu, 180001, India

    Dhiraj Vyas

Authors
  1. Arun Dev Sharma
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  2. Gurmeen Rakhra
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  3. Dhiraj Vyas
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Contributions

ADS and DV designed the study. GR carried out this work.

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Correspondence to Arun Dev Sharma.

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Sharma, A.D., Rakhra, G. & Vyas, D. Expression analysis and molecular modelling of hydrophilin LEA-2-like gene from wheat. Plant Physiol. Rep. 27, 160–170 (2022). https://doi.org/10.1007/s40502-021-00615-y

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  • DOI: https://doi.org/10.1007/s40502-021-00615-y

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