The Wheat Pathogenesis Related Protein (TdPR1.2) Ensures Contrasting Behaviors to <i>E. coli</i> Transformant Cells under Stress Conditions — Oak Academic Publishing
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The Wheat Pathogenesis Related Protein (TdPR1.2) Ensures Contrasting Behaviors to <i>E. coli</i> Transformant Cells under Stress Conditions
Biology Department, Faculty of Science, University of Ha’il, Ha’il, Saudi Arabia
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Biotechnology and Plant Improvement Laboratory, Centre of Biotechnology of Sfax (CBS), University of Sfax, Sfax, Tunisia
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Biology Department, Faculty of Science, University of Ha’il, Ha’il, Saudi Arabia
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Biology Department, Faculty of Science, University of Ha’il, Ha’il, Saudi Arabia
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Biology Department, Faculty of Science, University of Ha’il, Ha’il, Saudi Arabia
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Biotechnology and Plant Improvement Laboratory, Centre of Biotechnology of Sfax (CBS), University of Sfax, Sfax, Tunisia
1 Biology Department, Faculty of Science, University of Ha’il, Ha’il, Saudi Arabia
2 Biotechnology and Plant Improvement Laboratory, Centre of Biotechnology of Sfax (CBS), University of Sfax, Sfax, Tunisia
3 Biology Department, Faculty of Science, University of Ha’il, Ha’il, Saudi Arabia
4 Biology Department, Faculty of Science, University of Ha’il, Ha’il, Saudi Arabia
5 Biology Department, Faculty of Science, University of Ha’il, Ha’il, Saudi Arabia
6 Biotechnology and Plant Improvement Laboratory, Centre of Biotechnology of Sfax (CBS), University of Sfax, Sfax, Tunisia
The pathogenesis-related proteins 1 (PR-1) gene family play important roles in the plant metabolism in response to biotic and abiotic stresses. The wheat TdPR1.2 has been previously isolated and characterized. Here we showed by bio-informatic analysis that TdPR1.2 contains six cysteine residues that are conserved between all PR-1 proteins tested. Using ScanProsite tool, we found that TdPR1.2 structure has a CRISP family signature 1 and 2 located at the C-terminal part of the protein. Those two domains are conserved in many identified PR1.2 proteins in plants. Moreover, SignalIP-5.0 analysis revealed that TdPR1.2 contains a putative signal peptide formed by 25 amino acids at the N-terminal extremity. The presence of this signal peptide suggested that the mature proteins will be secreted after the cleavage of the signal sequence. Further, we investigate the role of the TdPR1.2 proteins in the growth of Escherichia coli transformants cells under different abiotic stresses. Our results showed that the full-length form of TdPR1.2 enhanced tolerance of E. coli against salt and osmotic stress but not to KCl. Moreover, TdPR1.2 protein confers bacterial tolerance to heavy metals in solid and liquid mediums. Based on these results, we suggest that the TdPR1.2 protein could play an important role in response to abiotic stress conditions.
KeywordsAbiotic StressBioinformatic AnalysisDurum Wheat<i>E. coli</i>Growth InhibitionPathogen Related ProteinsProtein Expression
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