DEHYDRIN PROFILES OF SOME IRANIAN MELON VARIETIES (Cucumis melo L. Merr) UNDER DROUGHT STRE SS CONDITIONS


Abstract

Dehydrins are proteins that play a role in the mechanism of drought tolerance. This study aimed at establishing dehydrin profile and accumulation in four local melon varieties of Iran: Mino, Dargazi, Saveii, and Semsori, as well as in a commercial variety Honeydew. Plants were treated with drought stress by adjusting the soil water content to 75, 50, 40, 30 and 20% of field capacity (FC) by withholding water. Water status of plants was monitored based on the seedling fresh weight (FW) and relative water content of leaves (RWC). Total protein content was extracted, then heat-stable protein (HSP) fraction was isolated for each variety and water stress treatment. After SDS-PAGE of HSP, Western blotting analysis was carried out with Anti-dehydrin rabbit (primary) and Goat anti rabbit (secondary) antibodies. ANOVA results showed that with decreasing FC below 75%, FW and RWC decreased, but these changes significantly varied among genotypes. On the basis of FW and RWC data under different drought stress treatments, the following drought-tolerant ranking was established: Mino > Dargazi > Saveii and Honeydew > Semsori, from tolerant to sensitive order. Results of Western blot analysis showed that expression of some proteins with molecular weights of 19–52 kDa was induced in the studied varieties under drought stress (% FC). Expression level of the dehydrin proteins in different varieties was variable and also depending on the drought stress level applied. However, dehydrin proteins (45 and 50 kDa) showed strong expression levels in all varieties under severe drought stress (20% FC). The abundance of dehydrin proteins was higher in tolerant varieties (Mino and Dargazi) than in moderate and drought sensitive genotypes. Consequently, dehydrins represent a potential marker for selection of genotypes with enhanced drought tolerance.


Keywords

melon; drought stress; dehydrin; western blotting

Arumingtyas, E.L., Widoretno, W., Indriyani, S. (2012). Somaclonal variations of soybeans (Glycine Max. L. Merr) stimulated by drought stress based on random amplified polymorphic DNAs (RAPDs). Am. J. Mol. Biol., 2, 85–91.
Arumingtyas, E.L., Savitri, E.S., Purwoningrahayu, R.D. (2013). Protein profiles and dehydrin accumulation in some soybean varieties (Glycine max L. Merr) in drought stress conditions. Am. J. Plant Sci., 4, 134–141.
Barrs, C., Weatherley, P.E. (1968). A re-examination of the relative turgidity technique for estimating water deficit in leaves. Austral. J. Biol. Sci., 15, 413–428.
Beck, E.H., Fettig, S., Knake, C., Hartig, K., Bhattarai, T. (2007). Specific and unspecific responses of plants to cold and drought stress. J. Biosci., 32, 501–510.
Bao, F., Du, D., Yang, A., Yang, W., Wang, J., Cheng, T., Zhang, O. (2017). Overexpression of Prunus mume dehydrin genes in tobacco enhances tolerance to cold and drought. Front. Plant Sci., 10, 1–6.
Bradford, M.M. (1976). A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein–dye binding. Anal. Biochem., 72, 248–254.
Cellier, F., Conéjéro, G., Breitler, J.C., Casse, F. (1998). Molecular and physiological responses to water deficit in drought-tolerant and drought-sensitive lines of sunflower. Accumulation of dehydrin transcripts correlates with tolerance. Plant Physiol., 116, 319–28.
Close, T.J. (1996). Dehydrin: emergence of a biochemical role of a family of plant dehydration proteins. Physiol. Plant, 97, 795–803.
Close, T.J. (1997). Dehydrins – a commonalty in the response of plants to dehydration and low temperature. Biol. Plant., 100, 291–296.
Close, T.J., Choi, D.W., Campbell, S.A., Koag, M.C., Zhu, B. (2000). The dehydrin multigene family in the Triticeae and maize. In: Molecular approaches for the genetic improvement of cereals for stable production in water-limited environments. A Strategic Planning Workshop, Ribaut, J.M., Poland, D.A. (eds.). CIMMYT, Mexico, D.F., Mexico, 167–170.
Fathi, A., Barari D.T. (2016). Effect of drought stress and its mechanism in plants. Int. J. Life Sci., 10, 1–6.
Hara, M., Fujinaga, M., Kuboi, T. (2004). Radical scavenging activity and oxidative modification of citrus dehydrin. Plant Physiol. Biochem., 42, 657–662.
Hara, M. (2009). The multifunctionality of dehydrins. An Overview. Plant Signal. Behav., 5, 503–508.
Houde, M., Dhindsa, R.S., Sarhan, F. (1992). A molecular marker to select for freezing tolerance in Gramineae. Mol. General Gen. MGG, 234, 43–48.
Jiang, Y., Huang, B. (2002). Protein alterations in response to water stress and ABA in tall fescue. Crop Sci., 42, 202–207.
Keyvan, S. (2010). The effects of drought stress on yield, relative water content, proline, soluble carbohydrates and chlorophyll of bread wheat varieties. J. Anim. Plant Sci., 8, 1051– 1060.
Korir, P., Nyabundi, J., Kimutro, P. (2006). Genotypic response of common bean (Phaseolus vulgaris L.) to moisture stress condition in Kenya. Asian J. Plant Sci., 5, 24–32.
Kumar, M., Lee, S.C., Kim, J.Y., Kim, S.S., Aye, S., Kim, S.R. (2014). Over-expression of dehydrin gene, OsDhn1, improves drought and salt stress tolerance through scavenging of reactive oxygen species in rice (Oryza sativa L.). J. Plant Biol., 57, 383–393.
Kuşvuran, A., Yıldız, H., Daşgan, B., Kazım, A. (2011). Responses of different melon genotypes to drought stress. YYU J. Agric. Sci., 21, 209–219.
Kyriakis, J.M., Banerjee, P., Nikolakaki, E., Dai, T., Rubie, E.A., Ahmad, M.F., Avruch, J., Woodgett, J.R. (1994). The stress-activated protein kinase subfamily of c-Jun kinases. Nature, 369, 156–160.
Lopez, C.G., Banowetz, G.M., Peterson, C.J., Kronstad, W.E. (2002). Wheat dehydrin accumulation in response to drought stress during anthesis. Plant Signal. Behav., 29, 1417–1425.
Lopez, C.G., Banowetz, G.M., Peterson, C.J., Kronstad, W.E. (2001). Differential accumulation of a 24-kDa dehydrin protein in wheat seedlings correlates with drought stress tolerance at grain filling. Hereditas, 135, 175–181.
Mohammadkhani, N., Heidari, R. (2008). Effects of drought stress on soluble proteins in two maize varieties. Turk. J. Biol., 32, 23–30.
Ochoa-Alfaro, A.E., Rodríguez-Kessler, M., Pérez-Morales, M.B., Delgado-Sánchez, P., Cuevas-Velazquez, C.L., Gómez-Anduro, G., Jiménez-Bremont, J.F. (2012). Functional characterization of an acidic SK3 dehydrin isolated from an Opuntia streptacantha cDNA library. Planta, 235, 565–578.
Olave-Concha, N., Bravo, L.A., Ruiz-Lara, S., Corcuera, L.J. (2005). Differential accumulation of dehydrin-like proteins by abiotic stresses in Deschampsia antarctica Desv. Polar Biol., 28, 506–513.
Samarah, N.H., Mullen, R.E., Cianzio, S.R., Scott, P. (2006). Dehydrin-like protein in soybean seeds in response to drought stress during seed filling. Crop Sci., 46, 2141–2150.
Schonfeld, M.A., Johnson, R.C., Carver, B. F., Mornhinweg, D.W. (1988). Water relations in winter wheat as drought resistance indicators. Crop Sci., 28, 526–531.
Shetty, K., Ohshima, M., Marakami, T., Oosawa, K., Ohashi, Y. (1997). Transgenic melon (Cucumis melo L.) and potential for expression novel proteins important to food industry. Food Biotechnol., 11, 111–128.
Sinclair, T., Ludlow, M. (1985). Who taught plants thermodynamics? The unfulfilled potential of plant water potential. Aust. J. Plant Physiol., 12, 213–217.
Vaseva, I., Akiscan, Y., Demirevska, K., Anders, I., Feller, U. (2011). Drought stress tolerance of red and white clover e comparative analysis of some chaperonins and dehydrins. Sci. Hortic., 130, 653–659.
Volaire, F., Genevieve, C., Francois, L. (2001). Drought survival and dehydration tolerance in Dactylis glomerata and Poa bulbosa. Austral. J. Plant Physiol., 28, 743–754.
Download

Published : 2019-12-17


Motallebi-Azar, A., Papp, I., & Szegő, A. (2019). DEHYDRIN PROFILES OF SOME IRANIAN MELON VARIETIES (Cucumis melo L. Merr) UNDER DROUGHT STRE SS CONDITIONS. Acta Scientiarum Polonorum Hortorum Cultus, 18(6), 75-84. https://doi.org/10.24326/asphc.2019.6.8

Alireza Motallebi-Azar  motallebiazar@gmail.com
Department of Plant Physiology and Plant Biochemistry, Szent István University, Budapest, Hungary; Department of Horticultural Science, Faculty of Agriculture, University of Tabriz, Tabriz, Iran  Iran, Islamic Republic of
István Papp 
Department of Plant Physiology and Plant Biochemistry, Szent István University, Budapest, Hungary  Hungary
Anita Szegő 
Department of Plant Physiology and Plant Biochemistry, Szent István University, Budapest, Hungary  Hungary


CitedBy Crossref
0

CitedBy Scopus
0



Articles are made available under the CC BY-NC-ND (recognition by authorship, non-commercial use, no dependent works).
The author signs a statement on the originality of the work, the contribution of individuals and the transfer of copyright to the publisher.
Submission of the paper implies that it has not been published previously, that it is not under consideration for publication elsewhere, and that if accepted it will not be published elsewhere in the same form without the written permission of the editor.