Abstract
Hordeum spontaneum (wild barley) is a good gene source to improve salt tolerance in barley because it rapidly hybridizes and recombines with barley cultivars. Proteomics can assist in identifying proteins associated with a certain environmental or developmental signal. We employed a proteomic approach to understand the mechanisms of plant responses to salinity in a salt tolerant accession of H. spontaneum. At the 4-leaf stage, wild barley plants were exposed to 0 (control treatment) or 300 mM NaCl (salt treatment). The salt treatment lasted 3 weeks. Total proteins of leaf 4 were extracted and separated by two-dimensional gel electrophoresis. More than 500 protein spots were reproducibly detected. Of these, 29 spots showed significant differences between salt treatment and control. Using MALDI-TOF-TOF MS, we identified 29 cellular proteins, which represented 16 different proteins. These were classified into six categories and a group with unknown biological function. The proteins identified were involved in many different cellular functions. Three spots were identified as unknown proteins; searching in the NCBI database revealed that there was a 71% match with clathrin assembly protein putative [Ricinus communis], a 67% match with actin binding protein [Zea mays], and a 66% match with phosphatidylinositol kinase [Arabidopsis thaliana]. Other proteins identified included ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), oxygen-evolving enhancer protein (OEE), photosystem II reaction centerWprotein (Psbw), ribosomal proteins, chloroplast RNA binding protein (ChRBP), superoxide dismutase (SOD), malate dehydrogenase (MDH), thioredoxin h (Trx), nucleoside diphosphate kinase (NDPK), profilin, translationally-controlled tumor protein (TCTP), polyamine oxidase (PAO) and universal stress protein family (USP).
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Askari, H., Edqvist, J., Hajheidari, M., Kafi, M., Salekdeh, G.H. 2006. Effects of salinity levels on proteome of Suaeda aegyptiaca leaves. Proteomics 6:2542–2554.
Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-Dye binding. Anal. Biochem. 72:248–254.
Cooley, T., Walters, D.R., 2002. Polyamine metabolism in barley reacting hypersensitively to the powdery mildew fungus Blumeria graminis f. sp. Hordei. Plant Cell Environ. 25:461–468.
Dadashi Dooki, A., Mayer-Posne, F., Askari, H., Zaiee, A., Salekdeh, G.H. 2006. Proteomic responses of rice young panicles to salinity. Proteomics 6:6498–6507.
Damerval, C., de Vienne, D., Zivy, M., Thiellement, H. 1986. Technical improvements in two-dimensional electrophoresis increase the level of genetic variation detected in wheat-seedling proteins. Electrophoresis 7:52–54.
Escobar Galvis, M.L., Marttila, S., Hakansson, G., Forsberg, J., Knorpp, C. 2001. Heat stress response in pea involves interaction of mitochondrial nucleoside diphosphate kinase with a novel 86-kilodalton protein. Plant Physiol. 126:69–77.
Görg, A., Postel, W., Günther, S. 1988. The current state of two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis 9:531–546.
Groppa, M.D., Benavides, M.P. 2008. Polyamines and abiotic stress: recent advances. Amino Acids 34:35–45.
Hajduch, M., Rakwal, R., Agrawal, G.K., Yonekura, M., Pretova, A. 2001. High-resolution two-dimensional electrophoresis separation of proteins from metal-stressed rice (Oryza sativa L.) leaves: Drastic reductions/fragmentation of ribulose-1,5-bisphosphate carboxylase/oxygenase and induction of stress-related proteins. Electrophoresis 22:2824–2831.
Helena, S., Ake, S. 2004. A Pisum sativum glyoxysomal malate dehydrogenase induced by cadmium exposure. J. of DNA Sequencing and Mapping 15:206–208.
Janicka-Russak, M., Kabala, K., Mlodzinska, E., Klobus, G. 2010. The role of polyamines in the regulation of the plasma membrane and the tonoplast proton pumps under salt stress. J. Plant Physiol. 167:261–269.
Laloi, C., Mestres-Ortega, D., Marco, Y., Meyer, Y., Reichheld, J.P. 2004. The Arabidopsis cytosolic thioredoxin h5 gene induction by oxidative stress and its W-box-mediated response to pathogen elicitor. Plant Physiol. 134:1006–1016.
Leshem, Y., Seri, L., Levine, A. 2007. Induction of phosphatidylinositol 3-kinase-mediated endocytosis by salt stress leads to intracellular production of reactive oxygen species and salt tolerance. The Plant Journal 51:185–197.
Ma, Y., Cheng, Z., Wang, W., Sun, Y. 2007. Proteomic analysis of high yield rice variety mutated from spaceflight. Adv. Space Res. 40:535–539.
Mikami, K., Katagiri, T., Iuchi, S., Yamaguchi-Shinozaki, K., Shinozaki, K. 1998. A gene encoding phosphatidylinositol-4-phosphate 5-kinase is induced by water stress and abscisic acid in Arabidopsis thaliana. The Plant Journal 15:563–568.
Moon, H., Lee, B., Choi, G., Shin, D., Prasad, D.T., Lee, O., Kwak, S.S., Kim, D.H., Nam, J., Bahk, J., Hong, J.C., Lee, S.Y., Cho, M.J., Lim, C.O., Yun, D.J. 2003. NDP kinase 2 interacts with two oxidative stress-activated MAPKs to regulate cellular redox state and enhances multiple stress tolerance in transgenic plants. Proc. Natl. Acad. Sci. USA. 100:358–363.
Munns, R., Tester, M. 2008. Mechanisms of salinity tolerance. Ann. Rev. Plant Biol. 59:651–681.
Nevo, E., Krugman, T., Beiles, A. 1993. Genetic resources for salt tolerance in the wild progenitors of wheat (Triticum dicoccoides) and barley (Hordeum spontaneum) in Israel. Plant Breed. 110:338–341.
O’Toole, R., Williams, H.D. 2003. Universal stress proteins and Mycobacterium tuberculosis. Res. Microbiol. 154:387–392.
Salekdeh, G.H., Siopongco, J., Wade, L.J., Ghareyazie, B., Bennett, J. 2002. Proteomic analysis of rice leaves during drought stress and recovery. Proteomics 2:1131–1145.
Shavrukov, Y., Gupta, N., Miyazaki, J., Baho, M., Chalmers, K., Tester, M., Langridge, P., Collins, N. 2010. HvNax3 — a locus controlling shoot sodium exclusion derived from wild barley (Hordeum vulgare ssp. spontaneum). Funct. Integr. Genomics 10:277–291.
Sobhanian, H., Razavizadeh, R., Nanjo, Y., Ehsanpour, A., Rastgar Jazii, F., Motamed, N., Komatsu, S. 2010. Proteome analysis of soybean leaves, hypocotyls and roots under salt stress. Proteome Sci. 8:19–33.
Sottosanto, J.B., Gelli, A., Blumwald, E. 2004. DNA array analyses of Arabidopsis thaliana lacking a vacuolar Na+/H+ antiporter: Impact of AtNHX1 on gene expression. The Plant Journal 40:752–771.
Sreenivasulua, N., Grimma, B., Wobusa, U., Weschkea, W. 2000. Differential response of antioxidant compounds to salinity stress in salt-tolerant and salt-sensitive seedlings of foxtail millet (Setaria italica). Physiological Plantarum 109:435–442.
Sugihara, K., Hanagata, N., Dubinsky, Z., Baba, S., Karube, I. 2000. Molecular characterization of cDNA encoding oxygen evolving enhancer protein 1 increased by salt treatment in the mangrove Bruguiera gymnorrhiza. Plant Cell Physiol. 41:1279–1285.
Unanue, E.R., Ungewickell, E., Branton, D. 1981. The binding of clathrin triskelions to membranes from coated vesicles. Cell 26:439–446.
Uribe, R., Jay, D. 2009. A review of actin binding proteins: New perspectives. Mol. Biol. Rep. 36:21–125.
Visa, N. 2005. Actin in transcription. EMBO Rep. 6:218–219.
Witzel, K., Weidneri, A., Surabhi, G., Varsheney, R., Kunze, G.H., Bck-sorlin, G., Borneri, A., Mock, H. 2010. Comparative analysis of the grain proteome fraction in barley genotypes with contrasting salinity tolerance during germination. Plant Cell Environ. 33:211–222.
Zorb, C., Schmitt, S., Neeb, A., Karl, S., Linder, M., Schubert, S. 2004. The biochemical reaction of maize (Zea mays L.) to salt stress is characterized by a mitigation of symptoms and not by a specific adaptation. Plant Sci. 167:91–100.
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Communicated by A. Pécsváradi
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Fatehi, F., Hosseinzadeh, A., Alizadeh, H. et al. The Proteome Response of Hordeum spontaneum to Salinity Stress. CEREAL RESEARCH COMMUNICATIONS 41, 78–87 (2013). https://doi.org/10.1556/CRC.2012.0017
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DOI: https://doi.org/10.1556/CRC.2012.0017