Water Stress Response in Different <i>Jatropha curcas</i> Accessions from Different Geographical Zones of Botswana: Biochemical & Physiological Perceptive — Oak Academic Publishing
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Water Stress Response in Different <i>Jatropha curcas</i> Accessions from Different Geographical Zones of Botswana: Biochemical & Physiological Perceptive
Department of Biological Sciences, University of Botswana, Private Bag UB 00707, Gaborone, Botswana
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Department of Crop Science, Botswana University of Agriculture & Natural Resources, Gaborone, Botswana
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Department of Biological Sciences, University of Botswana, Private Bag UB 00707, Gaborone, Botswana
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Department of Biological Sciences, University of Botswana, Private Bag UB 00707, Gaborone, Botswana
1 Department of Biological Sciences, University of Botswana, Private Bag UB 00707, Gaborone, Botswana
2 Department of Crop Science, Botswana University of Agriculture & Natural Resources, Gaborone, Botswana
3 Department of Biological Sciences, University of Botswana, Private Bag UB 00707, Gaborone, Botswana
4 Department of Biological Sciences, University of Botswana, Private Bag UB 00707, Gaborone, Botswana
Jatropha curcas L. is one climate smart drought-resistant multipurpose plant with a variety of properties that have conjured interest all over the world due to its potential to produce biofuel. In this study, Jatropha curcas accessions were collected from three different climate zones of Botswana; Northern region (Maun), Central region (Mmadinare) and Southern region (Thamaga). These accessions were subjected to water stress to study their biochemical a nd physiological responses. Results showed that water stress increased malondialdehyde (MDA) content, electrolyte leakage a s well as proline content in all the accessions. It is worth-noting that Maun accession exhibited highest proline content, when subjected to water stress. Maun accession also displa yed less MAD and electrolyte leakage than the other two accessions, an indication of less perturbation to membranes under water stress. This could be att ributed in part, to its higher catalase and superoxide dismutase contents, which presumably prevented lipid peroxidation by mopping up reactive oxygen species. The slightly higher dry weights exhibited by Mmadinare and Maun accessio ns could be ascribed to their ability to maintain membrane integrity under water stress conditions. It can therefore be concluded that Maun and Mmadinare accessions can be grown under drought conditions commonly experienced in Botswana.
Zhang, Q.F. (2007) Strategies for Developing Green Super Rice. Proceedings of the National Academy of Sciences of the United States of America, 104, 16402-16409. https://doi.org/10.1073/pnas.0708013104
Rizwan, S. and Aftab, F. (2018) Morphological and Biochemical Responses of Jatropha curcas under Water Stress. International Journal of Agriculture and Biology, 20, 1929-1936.
Foyer, C. and Fletcher, J. (2001) Plant Antioxidants: Color me Healthy. Biologist, 48, 115-120.
Gaschler, M. and Stockwell, B. (2017) Lipid Peroxidation in Cell Death. Biochemical and Biophysical Research Communications, 482, 419-425. https://doi.org/10.1016/j.bbrc.2016.10.086
Dat, J., Vandenabeele, S., Vranova, E., Van Montagu, M., Fuze, D. and Van Breusegem, F. (2000) Dual Action of the Active Oxygen Species during Plant Stress Responses. Cellular and Molecular Life Sciences, 57, 779-795. https://doi.org/10.1007/s000180050041
Chaves, M., Maroco, J.P. and Pereira, J.S. (2003) Understanding Plant Responses to Drought-From Genes to the Whole Plant. Functional Plant Biology, 30, 239-264. https://doi.org/10.1071/FP02076
Medeiros, D.B., Santos, H.R., Pacheco, C.M., Musser, R. and Nogueira, R.J. (2012) Physiological and Biochemical Responses of Drought Stress in Barbados Cherry. Brazilian Society of Plant Physiology, 24, 181-192. https://doi.org/10.1590/S1677-04202012000300005
Sharma, S., Dhamija, H.K. and Parashar, B. (2012) Jatropha curcas: A Review. Asian Pharmacy, 2, 101-111.
Islam, A.K., Yaakob, Z. and Anuar, N. (2011) Jatropha: A Multipurpose Plant with Considerable Potential for the Tropics. Scientific Research and Essays, 6, 2597-2605.
Moseki, B. and Dintwe, K. (2011) Effect of Water Stress on Photosynthetic Characteristics of Two Sorghum Cultivars. The African Journal of Plant Sciences and Biotechnology, 5, 89-91.
Heath, R. and Packer, L. (1968) Photoperoxidation in Isolated Chloroplasts: I. Kinetics and Stoichiometry on Fatty Acid Peroxidation. Archives in Biochemistry and Biophysics, 125, 189-198. https://doi.org/10.1016/0003-9861(68)90654-1
Hodges, D., DeLong, J., Forney, C. and Prange, R. (1999) Improving the Thiobarbituric Acid Reactive Substances Assay for estimating Lipid Peroxidation in Plant Tissues Containing Anthocyanin and Other Interfering Compounds. Planta, 207, 604-611. https://doi.org/10.1007/s004250050524
Lutts, S., Kinet, J. and Bouharmont, J. (1996) NaCl-Induced Senescence in Leaves of Rice (Oryza sativa L.) Cultivars Differing in Salinity Resistance. Annals of Botany, 78, 389-398. https://doi.org/10.1006/anbo.1996.0134
Giannopolitis, C.N. and Ries, S.K. (1977) Superoxide Dismutases: Occurrence in Higher Plants. Plant Physiology, 59, 309-314. https://doi.org/10.1104/pp.59.2.309
Zhang, C., Bruins, M.E., Yang, Z., Liu, S. and Rao, P. (2016) A New Formula to Calculate Activity of Superoxide Dismutase in Indirect Assays. Analytical Biochemistry, 503, 65-67. https://doi.org/10.1016/j.ab.2016.03.014
Kar, M. and Mishra, D. (1976) Catalase, Peroxidase, and Polyphenoloxidase Activities during Rice Leaf Senescence. Plant Physiology, 57, 315-319. https://doi.org/10.1104/pp.57.2.315
Senthilkumar M., Amaresan N. and Sankaranarayanan A. (2021) Plant-Microbe Interactions. Springer Protocols Handbooks, New York. https://doi.org/10.1007/978-1-0716-1080-0
Bates, L.S., Waldren, R.P. and Teare, I.D. (1973) Rapid Determination of Free Proline for Water-Stress Studies. Plant and Soil, 39, 205-207. https://doi.org/10.1007/BF00018060
Lowry, O.H., Rosebrough, N.J., Farr, A.L. and Randall, R.J. (1951) Protein Measurement with the Folin Phenol Reagent. Journal of Biological Chemistry, 193, 265-275. https://doi.org/10.1016/S0021-9258(19)52451-6
Nadia, K. and Naqvi, F.N. (2010) Effect of Water Stress on Lipid Peroxidation and Antioxidant Enzymes in Local Bread Wheat Hexaploids. Journal of Food, Agriculture and Environment, 8, 521-526.
Mouradi, M., Farissi, M., Bouizgaren, A., Lahrizi, Y., Qaddoury, A. and Ghoulam, C. (2018) Alfalfa and Its Symbiosis Responses to Osmotic Stress. In: Bezerra, R.L., Ed., New Perspectives in Forage Crops, Intech Open, Morocco, 150-168. https://doi.org/10.5772/intechopen.69760
Esfandiari, E.O., Shakiba, M.R., Mahboob, S.A., Alyari, H. and Toorchi, M. (2007) Water Stress, Antioxidant Enzyme Activity and Lipid Peroxidation in Wheat Seedling. Journal of Food, Agriculture and Environment, 5, 149-153.
Lismont, C., Revenco, I. and Fransen, M. (2019) Peroxisomal Hydrogen Peroxide Metabolism and Signaling in Health and Disease. International Journal of Molecular Sciences, 20, 1-20. https://doi.org/10.3390/ijms20153673
Laxa, M., Liebthal, M., Telman, W., Chibani, K. and Dietz, K.J. (2019) The Role of the Plant Antioxidant System in Drought Tolerance. Antioxidants, 8, 1-31. https://doi.org/10.3390/antiox8040094
Ashraf, M.F.M.R. and Foolad, M.R. (2007) Roles of Glycine Betaine and Proline in Improving Plant Abiotic Stress Resistance. Environmental and Experimental Botany, 59, 206-216. https://doi.org/10.1016/j.envexpbot.2005.12.006
Close, T.J. (1996) Dehydrins: Emergence of a Biochemical Role of a Family of Plant Dehydration Proteins. Physiologia Plantarum, 97, 795-803. https://doi.org/10.1111/j.1399-3054.1996.tb00546.x
Carpenter J.F. and Crowe J.H. (1988) The Mechanism of Cryoprotection of Proteins by Solutes. Cryobiology, 25, 244-255. https://doi.org/10.1016/0011-2240(88)90032-6
Dure, L., Crouch M., Harada, J., Ho, T.H., Mundy, J., Quatrano, R., Thomas, T. and Sung, Z.R. (1989) Common Amino Acid Sequence Domains among the LEA Proteins of Higher Plants. Plants Molecular Biology, 12, 475-486. https://doi.org/10.1007/BF00036962
Doke, N. (1997) The Oxidative Burst: Role in Signal Transduction and Plant Stress. In: Scandalios, J.G., Ed., Oxidative Stress and the Molecular Biology of Antioxidant Defenses, Cold Spring Harbor Press, New York.
Li, D., Li, C., Sun, H., Wang, W., Liu, L. and Zhang, Y. (2010) Effects of Drought on Soluble Protein Content and Protective Enzyme System in Cotton Leaves. Frontiers of Agriculture in China, 4, 56-62. https://doi.org/10.1007/s11703-010-0102-2
Surendar, K.K., Devi, D.D., Ravi, I., Jeyakumar, P. and Velayudham, K. (2013) Effect of Water Stress on Leaf Temperature, Transpiration Rate, Stomatal Diffusive Resistance and Yield of Banana. Plant Gene and Trait, 4, 43-47. https://doi.org/10.5376/pgt.2013.04.0008
Rodiyati, A., Arisoesilaningsih, E., Isagi, Y. and Nakagoshi, N. (2005) Responses of Cyperus brevifolius (Rottb.) Hassk. and Cyperus kyllingia Endl. to Varying Soil Water Availability. Environmental and Experimental Botany, 53, 259-269. https://doi.org/10.1016/j.envexpbot.2004.03.018
de Oliveira, M.V.A., Alves, D.D.L., de Morais Lima, L.H.G., de Castro Sousa, J.M. and Peron, A.P. (2013) Cytotoxicity of Erythrosine (E-127), Brilliant Blue (E-133) and Red 40 (E-129) Food Dyes in a Plant Test System. Acta Scientiarum, 35, 557-562. https://doi.org/10.4025/actascibiolsci.v35i4.18419