Abstract
Drought stress modulates the expression levels of numerous stress responsive genes which are not yet independently characterized in detail. Isolation and molecular characterization of the novel genes is necessary to understand plant stress physiology and to engineer stress resistant crops. In this study, two drought responsive genes, wheat cold-regulated gene 410c (WCOR410C) and Triticum aestivum Ring Finger 1 (TaRF1), previously implicated in protective roles were selected for characterization. Four bread wheat cultivars (CV) were analyzed for their response towards drought. CV such as NARC and Td-1 appeared as more drought tolerant with less drop in relative water content. Moreover, upon exposure to dehydration stress, differential expression was observed for WCOR410C, a dehydrin gene. However, cultivars tolerance emerged as a function of drought intensity. TaRF1, a ubiquitin ligase, showed drought dependent fourth intron retention in the cultivar Td-1 illustrating the effect of drought stress on the spilceosomal machinery. It is suggested that splicing events giving rise to transcriptome/proteome diversity might play dynamic role in plant’s adaptation to drought stress. Additionally, structural models were predicted for dehydrin domain of WCOR410C and RING-finger domain of TaRF1.
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Barrs H, Weatherley P (1962) A re-examination of the relative turgidity technique for estimating water deficits in leaves. Aust J Biol Sci 15:413. https://doi.org/10.1071/BI9620413
Chasapis C, Spyroulias G (2009) RING finger E3 ubiquitin ligases: structure and drug discovery. Curr Pharm Des 15:2. https://doi.org/10.2174/138161209789271825
Cristobal S, Zemla A, Fischer D et al (2001) A study of quality measures for protein threading models. BMC Bioinform 1:2–3. https://doi.org/10.1186/1471-2105-2-5
Cutler SR, Rodriguez PL, Finkelstein RR, Abrams SR (2010) Abscisic acid: emergence of a core signaling network. Annu Rev Plant Biol. https://doi.org/10.1146/annurev-arplant-042809-112122
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. Plant Cell. https://doi.org/10.1105/tpc.10.4.623
DeLano WL (2002) The PyMOL molecular graphics system. Schrödinger LLC wwwpymolorg Version 1.: http://www.pymol.org. citeulike-article-id: 240061
Guerra D, Mastrangelo AM, Lopez-Torrejon G et al (2011) Identification of a protein network interacting with TdRF1, a wheat RING ubiquitin ligase with a protective role against cellular dehydration. Plant Physiol. https://doi.org/10.1104/pp.111.183988
Guerra D, Mastrangelo AM, Lopez-Torrejon G et al (2012) Identification of a protein network interacting with TdRF1, a wheat RING ubiquitin ligase with a protective role against cellular dehydration. Plant Physiol 158:777–789. https://doi.org/10.1104/pp.111.183988
Hassan NM, El-Bastawisy ZM, El-Sayed AK et al (2015) Roles of dehydrin genes in wheat tolerance to drought stress. J Adv Res 6:179–188. https://doi.org/10.1016/j.jare.2013.11.004
Källberg M, Wang H, Wang S et al (2012) Template-based protein structure modeling using the RaptorX web server. Nat Protoc 7:1511–1522. https://doi.org/10.1038/nprot.2012.085
Katoh S, Hong C, Tsunoda Y et al (2003) High precision NMR structure and function of the RING-H2 finger domain of EL5, a rice protein whose expression is increased upon exposure to pathogen-derived oligosaccharides. J Biol Chem 278:15341–15348. https://doi.org/10.1074/jbc.M210531200
Kelley LA, Sternberg MJE (2009) Protein structure prediction on the web: a case study using the phyre server. Nat Protoc 4:363–373. https://doi.org/10.1038/nprot.2009.2
Khan F, Sultana T, Deeba F, Saqlan Naqvi SM (2013) Dynamics of mRNA of glycine-rich RNA-binding protein during wounding, cold and salt stresses in Nicotiana tabacum. Pakistan J Bot 45:297–300
Khoury GA, Tamamis P, Pinnaduwage N et al (2014) Princeton_TIGRESS: protein geometry refinement using simulations and support vector machines. Proteins Struct Funct Bioinform 82:794–814. https://doi.org/10.1002/prot.24459
Kundu S, Gantait S (2017) Abscisic acid signal crosstalk during abiotic stress response. Plant Gene 1:2–3. https://doi.org/10.1016/j.plgene.2017.04.007
Laskowski RA, MacArthur MW, Moss DS, Thornton JM (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Crystallogr 26:283–291. https://doi.org/10.1107/S0021889892009944
Li Z, Cao R, Wang M et al (2006) Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex. J Biol Chem 281:20643–20649. https://doi.org/10.1074/jbc.M602461200
Lim CW, Park C, Kim J et al (2017) Pepper CaREL1, a ubiquitin E3 ligase, regulates drought tolerance via the ABA-signalling pathway. Sci Rep. https://doi.org/10.1038/s41598-017-00490-4
Livak KJ, Schmittgen TD (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods 25:402–408. https://doi.org/10.1006/meth.2001.1262
Mastrangelo AM, Belloni S, Barilli S et al (2005) Low temperature promotes intron retention in two e-cor genes of durum wheat. Planta 221:705–715. https://doi.org/10.1007/s00425-004-1475-3
Metzger MB, Pruneda JN, Klevit RE, Weissman AM (2014) RING-type E3 ligases: master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination. Biochim Biophys Acta Mol Cell Res 1843:47–60
Nakashima K, Yamaguchi-Shinozaki K (2013) ABA signaling in stress-response and seed development. Plant Cell Rep 32(7):959–970
Park SY, Noh KJ, Yoo JH et al (2006) Rapid upregulation of Dehyrin3 and Dehydrin4 in response to dehydration is a characteristic of drought-tolerant genotypes in barley. J Plant Biol 49:455–462. https://doi.org/10.1007/BF03031126
Raghavendra AS, Gonugunta VK, Christmann A, Grill E (2010) ABA perception and signalling. Trends Plant Sci 15(7):395–401
Rajesh S, Manickam A (2006) Prediction of functions for two LEA proteins from mung bean. Bioinformation 1:133–138
Rock CD (2000) Pathways to abscisic acid-regulated gene expression. New Phytol 148:357–396
Shewry PR, Hey SJ (2015) The contribution of wheat to human diet and health. Food Energy Secur 4(3):178–202
Soltys-kalina D, Marczewski W (2016) The effect of drought stress on the leaf relative water content and tuber yield of a half-sib family of ‘Katahdin’-derived potato cultivars. Breed Sci 66:328–331. https://doi.org/10.1270/jsbbs.66.328
Verma V, Ravindran P, Kumar PP (2016) Plant hormone-mediated regulation of stress responses. BMC Plant Biol. https://doi.org/10.1186/s12870-016-0771-y
Wasilewska A, Vlad F, Sirichandra C et al (2008) An update on abscisic acid signaling in plants and more ···. Mol Plant 1(2):198–217
Wiederstein M, Sippl MJ (2007) ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins. Nucleic Acids Res. https://doi.org/10.1093/nar/gkm290
Wolkers WF, McCready S, Brandt WF et al (2001) Isolation and characterization of a D-7 LEA protein from pollen that stabilizes glasses in vitro. Biochim Biophys Acta Protein Struct Mol Enzymol 1544:196–206. https://doi.org/10.1016/S0167-4838(00)00220-X
Wu S, Zhang Y (2007) LOMETS: a local meta-threading-server for protein structure prediction. Nucleic Acids Res 35:3375–3382. https://doi.org/10.1093/nar/gkm251
Yang J, Yan R, Roy A et al (2014) The I-TASSER suite: protein structure and function prediction. Nat Methods 12:7–8. https://doi.org/10.1038/nmeth.3213
Zhang J, Jia W, Yang J, Ismail AM (2006) Role of ABA in integrating plant responses to drought and salt stresses. Field Crops Res 97(1):111–119
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This research was funded by the Higher Education Commission (HEC) Pakistan.
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Kiani, I., Naqvi, S.M.S., Sultana, T. et al. Characterization of two novel drought responsive genes in wheat. J. Plant Biochem. Biotechnol. 29, 78–85 (2020). https://doi.org/10.1007/s13562-019-00514-2
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DOI: https://doi.org/10.1007/s13562-019-00514-2