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1.
Plant Physiol Biochem ; 97: 420-31, 2015 Dec.
Article in English | MEDLINE | ID: mdl-26555900

ABSTRACT

Catalases are reactive oxygen species scavenging enzymes involved in response to abiotic and biotic stresses. In this study, we described the isolation and functional characterization of a novel catalase from durum wheat, designed TdCAT1. Molecular Phylogeny analyses showed that wheat TdCAT1 exhibited high amino acids sequence identity to other plant catalases. Sequence homology analysis showed that TdCAT1 protein contained the putative calmodulin binding domain and a putative conserved internal peroxisomal targeting signal PTS1 motif around its C-terminus. Predicted three-dimensional structural model revealed the presence of four putative distinct structural regions which are the N-terminal arm, the ß-barrel, the wrapping and the α-helical domains. TdCAT1 protein had the heme pocket that was composed by five essential residues. TdCAT1 gene expression analysis showed that this gene was induced by various abiotic stresses in durum wheat. The expression of TdCAT1 in yeast cells and Arabidopsis plants conferred tolerance to several abiotic stresses. Compared with the non-transformed plants, the transgenic lines maintained their growth and accumulated more proline under stress treatments. Furthermore, the amount of H2O2 was lower in transgenic lines, which was due to the high CAT and POD activities. Taken together, these data provide the evidence for the involvement of durum wheat catalase TdCAT1 in tolerance to multiple abiotic stresses in crop plants.


Subject(s)
Adaptation, Physiological , Arabidopsis/physiology , Catalase/metabolism , Saccharomyces cerevisiae/physiology , Stress, Physiological , Transformation, Genetic , Triticum/enzymology , Adaptation, Physiological/genetics , Amino Acid Sequence , Antioxidants/metabolism , Arabidopsis/genetics , Catalase/chemistry , Catalase/genetics , Gene Expression Regulation, Plant , Hydrogen Peroxide/metabolism , Phylogeny , Plant Proteins/chemistry , Plant Proteins/genetics , Plant Proteins/metabolism , Plants, Genetically Modified , Proline/metabolism , RNA, Messenger/genetics , RNA, Messenger/metabolism , Saccharomyces cerevisiae/genetics , Sequence Analysis, Protein , Stress, Physiological/genetics
2.
Planta ; 242(5): 1187-94, 2015 Nov.
Article in English | MEDLINE | ID: mdl-26105651

ABSTRACT

MAIN CONCLUSION: The wheat dehydrin (DHN-5) gives birth to salinity tolerance to transgenic Arabidopsis plants by the regulation of proline metabolism and the ROS scavenging system. Dehydrins (DHNs) are involved in plant abiotic stress tolerance. In this study, we reported that salt tolerance of transgenic Arabidopsis plants overexpressing durum wheat dehydrin (DHN-5) was closely related to the activation of the proline metabolism enzyme (P5CS) and some antioxidant biocatalysts. Indeed, DHN-5 improved P5CS activity in the transgenic plants generating a significant proline accumulation. Moreover, salt tolerance of Arabidopsis transgenic plants was accompanied by an excellent activation of antioxidant enzymes like catalase (CAT), superoxide dismutase (SOD) and peroxide dismutase (POD) and generation of a lower level of hydrogen peroxide (H2O2) in leaves compared to the wild-type plants. The enzyme activities were enhanced in these transgenic plants in the presence of exogenous proline. Nevertheless, proline accumulation was slightly reduced in transgenic plants promoting chlorophyll levels. All these results suggest the crucial role of DHN-5 in response to salt stress through the activation of enzymes implicated in proline metabolism and in ROS scavenging enzymes.


Subject(s)
Arabidopsis/drug effects , Arabidopsis/metabolism , Plant Proteins/physiology , Plants, Genetically Modified/drug effects , Plants, Genetically Modified/metabolism , Proline/metabolism , Salt Tolerance/genetics , Triticum/genetics , Arabidopsis/genetics , Gene Expression Regulation, Plant/drug effects , Gene Expression Regulation, Plant/genetics , Plant Proteins/genetics , Plants, Genetically Modified/genetics , Reactive Oxygen Species/metabolism , Salts/pharmacology
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