Proteomic Investigations to Assess the Impact of Salinity on Vigna radiata L. Genotypes

Author(s): Hesham F. Alharby, Khalid Rehman Hakeem*

Journal Name: Current Proteomics

Volume 18 , Issue 2 , 2021


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Abstract:

Background: In our previous study, six cultivars of Mungo (Vigna radiata) were exposed to 100-250 mM NaCl and studied for changes in growth and biomass. Among them, AEM-96 cultivar of the Mung bean [Vigna radiata (L.) Wilczek cv.] was found to tolerate NaCl stress at 250 mM.

Objective: The soluble proteome of salt-tolerant mungo cultivar (AEM-96) was compared to the proteome of control mungo to investigate the possible mechanism of salinity tolerance.

Methods: Gel-based two-dimensional gel electrophoresis was employed for comparative proteomics. PDQuest-based image analysis of 2D SDS-PAGE was performed. Scatter plots were prepared and total spots were analyzed for 2-fold changes in abundance of protein spot intensities in control and treated gels.

Results: In total 517 protein spots were detected; 36 with high significance. Among these 36 spots, 2-fold expression change was analyzed in 27 protein spots. Seven protein spots were upregulated, eight spots were down-regulated, 3 spots were newly induced and 9 spots were silenced, while 9 protein spots did not change their 2-fold abundance under salinity. Protein spots (9 in total) which were 2-fold upregulated and newly induced were excised from the respective gels. The spots were tryptically digested and run on LC-MS/MS for generating peptides and performing a comparative fingerprinting of the proteins. The peptide signal data was loaded on the Mascot (Swissprot) database to retrieve protein IDs. Proteins with the best score were selected, namely isomers of oxygen- evolving enhancer protein 1 (S1-S3), RuBisCO (S4), oxygen-evolving enhancer protein 2 (S5), Heat shock protein 70 isomers (S6-S7), RuBisCO activase (S8), rubber elongation factor (S9) and pathogen-related protein 10 (S10).

Conclusion: The identified proteins were found to play important roles in photosynthesis, stress response and plant growth.

Keywords: Vigna mungo, salinity, proteomics, tolerance, LC-MS/MS, plant growth.

[1]
Yi-Shen, Z.; Shuai, S.; FitzGerald, R. Mung bean proteins and peptides: Nutritional, functional and bioactive properties. Food Nutr. Res., 2018, 62, 62.
[http://dx.doi.org/10.29219/fnr.v62.1290] [PMID: 29545737]
[2]
Sehrawat, N.; Yadav, M.; Sharma, A.K.; Kumar, V.; Jaiwal, P.K.; Bhat, K.V.; Sairam, R.K. Seedling vigor: an important criterion for the selection of salt tolerant lines for mungbean (Vigna radiata (L.) Wilczek). Thai J. Agric. Sci., 2018, 51(3), 119-132.
[3]
Hussain, S.J.; Masood, A.; Anjum, N.A.; Khan, N.A. Sulfur-mediated control of salinity impact on photosynthesis and growth in mungbean cultivars screened for salt tolerance involves glutathione and proline metabolism, and glucose sensitivity. Acta Physiol. Plant., 2019, 41(8), 129.
[http://dx.doi.org/10.1007/s11738-019-2926-6]
[4]
Kalaiyarasi, S.; Avudaithai, S.; Somasundaram, S.; Sundar, M. Effect of INM on chemical properties of soil, nutrient uptake and yield of green gram in sodic soil. IJCS, 2019, 7(3), 2053-2055.
[5]
Lotfi, R.; Ghassemi-Golezani, K.; Najafi, N. Grain filling and yield of mung bean affected by salicylic acid and silicon under salt stress. J. Plant Nutr., 2018, 41(14), 1778-1785.
[http://dx.doi.org/10.1080/01904167.2018.1457686]
[6]
Alharby, H.F.; Al-Zahrani, H.S.; Hakeem, K.R. Salinity-induced antioxidant enzyme system in mungbean ([ Vigna radiata (L.) WILCZEK] CV.) genotypes. Pak. J. Bot., 2019, 51(4), 1191-1198.
[http://dx.doi.org/10.30848/PJB2019-4(13)]
[7]
Hapsari, R.T.; Trustinah, T. Salinity tolerance of mungbean genotypes at seedling stage. Biosaintifika: J. Biol. Biol. Edu., 2018, 10(2), 408-415.
[http://dx.doi.org/10.15294/biosaintifika.v10i2.13999]
[8]
Hoque, T.S.; Burritt, D.J.; Hossain, M.A. The glyoxalase system: A possible target for production of salinity-tolerant crop plants. Salinity Responses Tolerance Plants, 2018, 1, 257-281.
[http://dx.doi.org/10.1007/978-3-319-75671-4_10]
[9]
Alharby, H.F.; Al-Zahrani, H.S.; Hakeem, K.R.; Iqbal, M. Identification of physiological and biochemical markers for salt (NaCl) stress in the seedlings of mungbean [Vigna radiata (L.) Wilczek] genotypes. Saudi J. Biol. Sci., 2019, 26(5), 1053-1060.
[http://dx.doi.org/10.1016/j.sjbs.2018.08.006] [PMID: 31303840]
[10]
Hoagland, D.R.; Arnon, D.I. The water-culture method for growing plants without soil. Circular. California Agricult. Exp. Station, 1950, 347.
[11]
Molloy, M.P.; Witzmann, F.A. Proteomics: technologies and applications. Brief. Funct. Genomics Proteomics, 2002, 1(1), 23-39.
[http://dx.doi.org/10.1093/bfgp/1.1.23] [PMID: 15251064]
[12]
Shevchenko, A.; Loboda, A.; Shevchenko, A.; Ens, W.; Standing, K.G. MALDI quadrupole time-of-flight mass spectrometry: a powerful tool for proteomic research. Anal. Chem., 2000, 72(9), 2132-2141.
[http://dx.doi.org/10.1021/ac9913659] [PMID: 10815976]
[13]
Hanumantha, R.B.; Nair, R.M.; Nayyar, H.; Standing, K.G. Salinity and high temperature tolerance in mungbean [Vigna radiata (L.) Wilczek] from a physiological perspective. Front. Plant Sci., 2016, 7, 957-967.
[http://dx.doi.org/10.3389/fpls.2016.00957] [PMID: 27446183]
[14]
Hakeem, K.R.; Chandna, R.; Ahmad, P.; Iqbal, M.; Ozturk, M. Relevance of proteomic investigations in plant abiotic stress physiology. OMICS, 2012, 16(11), 621-635.
[http://dx.doi.org/10.1089/omi.2012.0041] [PMID: 23046473]
[15]
Bowes, G. Growth at elevated CO2: Photosynthetic responses mediated through Rubisco. Plant Cell Environ., 1991, 14(8), 795-806.
[http://dx.doi.org/10.1111/j.1365-3040.1991.tb01443.x]
[16]
Tine, M.; Bonhomme, F.; McKenzie, D.J.; Durand, J.D. Differential expression of the heat shock protein Hsp70 in natural populations of the tilapia, Sarotherodon melanotheron, acclimatised to a range of environmental salinities. BMC Ecol., 2010, 10(1), 11.
[http://dx.doi.org/10.1186/1472-6785-10-11] [PMID: 20429891]
[17]
Mazzucotelli, E.; Mastrangelo, A.M.; Crosatti, C.; Guerra, D.; Stanca, A.M.; Cattivelli, L. Abiotic stress response in plants: when post-transcriptional and post-translational regulations control transcription. Plant Sci., 2008, 174(4), 420-431.
[http://dx.doi.org/10.1016/j.plantsci.2008.02.005]
[18]
Wang, W.; Vinocur, B.; Shoseyov, O.; Altman, A. Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response. Trends Plant Sci., 2004, 9(5), 244-252.
[http://dx.doi.org/10.1016/j.tplants.2004.03.006] [PMID: 15130550]
[19]
Becker, J.; Craig, E.A. Heat-shock proteins as molecular chaperones. Eur. J. Biochem., 1994, 219(1-2), 11-23.
[http://dx.doi.org/10.1111/j.1432-1033.1994.tb19910.x] [PMID: 8306977]
[20]
Chen, S.; Smith, D.F. Hop as an adaptor in the Heat shock protein 70 (Hsp70) and hsp90 chaperone machinery. J. Biol. Chem., 1998, 273(52), 35194-35200.
[http://dx.doi.org/10.1074/jbc.273.52.35194] [PMID: 9857057]
[21]
Eissa, N.; Wang, H.P.; Yao, H.; Shen, Z.G.; Shaheen, A.A.; Abou-ElGheit, E.N. Expression of Hsp70, Igf1, and three oxidative stress biomarkers in response to handling and salt treatment at different water temperatures in yellow perch, Perca flavescens. Front. Physiol., 2017, 8, 683.
[http://dx.doi.org/10.3389/fphys.2017.00683] [PMID: 28955246]
[22]
Qureshi, M.I.; Muneer, S.; Bashir, H.; Ahmad, J.; Iqbal, M. Nodule physiology and proteomics of stressed legumes. Adv. Bot. Res., 2010, 56, 1-48.
[http://dx.doi.org/10.1016/B978-0-12-381518-7.00001-7]
[23]
Dennis, M.S.; Henzel, W.J.; Bell, J.; Kohr, W.; Light, D.R. Amino acid sequence of rubber elongation factor protein associated with rubber particles in Hevea latex. J. Biol. Chem., 1989, 264(31), 18618-18626.
[PMID: 2808390]
[24]
Sels, J.; Mathys, J.; De Coninck, B.M.; Cammue, B.P.; De Bolle, M.F. Plant Pathogenesis-Related (PR) proteins: A focus on PR peptides. Plant Physiol. Biochem., 2008, 46(11), 941-950.
[http://dx.doi.org/10.1016/j.plaphy.2008.06.011] [PMID: 18674922]
[25]
Mogk, A.; Bukau, B.; Kampinga, H.H. Cellular handling of protein aggregates by disaggregation machines. Mol. Cell, 2018, 69(2), 214-226.
[http://dx.doi.org/10.1016/j.molcel.2018.01.004] [PMID: 29351843]
[26]
Wienkoop, S.; Saalbach, G. Proteome analysis. Novel proteins identified at the peribacteroid membrane from Lotus japonicusroot nodules. Plant Physiol., 2003, 131(3), 1080-1090.
[http://dx.doi.org/10.1104/pp.102.015362] [PMID: 12644660]


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Article Details

VOLUME: 18
ISSUE: 2
Year: 2021
Published on: 19 April, 2020
Page: [106 - 112]
Pages: 7
DOI: 10.2174/1570164617999200420075125

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