The Putative Auto-Inhibitory Domain of Durum Wheat Catalase (TdCAT1) Positively Regulates Bacteria Cells in Response to Different Stress Conditions
Catalase is a crucial enzyme in the antioxidant defense system protecting organisms from oxidative stress. Proteins of this kind play important roles in controlling plant response to biotic and abiotic stresses by catalyzing the decomposition of H<sub>2</sub>O<sub>2</sub>. Th...
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MDPI AG
2022-09-01
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author | Mouna Ghorbel Kaouthar Feki Sana Tounsi Nouha Bouali Malek Besbes Faiçal Brini |
author_facet | Mouna Ghorbel Kaouthar Feki Sana Tounsi Nouha Bouali Malek Besbes Faiçal Brini |
author_sort | Mouna Ghorbel |
collection | DOAJ |
description | Catalase is a crucial enzyme in the antioxidant defense system protecting organisms from oxidative stress. Proteins of this kind play important roles in controlling plant response to biotic and abiotic stresses by catalyzing the decomposition of H<sub>2</sub>O<sub>2</sub>. The durum wheat catalase 1, TdCAT1, has been previously isolated and characterized. Here, using bio-informatic analysis, we showed that durum wheat catalase 1 TdCAT1 harbors different novel conserved domains. In addition, TdCAT1 contains various phosphorylation residues and S-Nitrosylation residues located at different positions along the protein sequence. TdCAT1 activity decreased after treatment with λ−phosphatase. On the other hand, we showed that durum wheat catalase 1 (TdCAT1) exhibits a low CAT activity in vitro, whereas a deleted form of TdCAT1 has better activity compared to the full-length protein (TdCAT460), suggesting that TdCAT1 could present a putative autoinhibitory domain in its C-terminal portion. Moreover, we showed that TdCAT1 positively regulates <i>E. coli</i> cells in response to salt, ionic and osmotic stresses as well as heavy metal stress in solid and liquid mediums. Such effects had not been reported and lead us to suggest that the durum wheat catalase 1 TdCAT1 protein could play a positive role in response to a wide array of abiotic stress conditions. |
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spelling | doaj.art-ed51c4b26cbc4c7b9d53ae2a264afbcb2023-11-23T14:49:27ZengMDPI AGAntioxidants2076-39212022-09-01119182010.3390/antiox11091820The Putative Auto-Inhibitory Domain of Durum Wheat Catalase (TdCAT1) Positively Regulates Bacteria Cells in Response to Different Stress ConditionsMouna Ghorbel0Kaouthar Feki1Sana Tounsi2Nouha Bouali3Malek Besbes4Faiçal Brini5Department of Biology, College of Sciences, University of Hail, P.O. Box 2440, Ha’il City 81451, Saudi ArabiaLaboratory of Biotechnology and Plant Improvement, Center of Biotechnology of Sfax, P.O. Box 1177, Sfax 3018, TunisiaLaboratory of Biotechnology and Plant Improvement, Center of Biotechnology of Sfax, P.O. Box 1177, Sfax 3018, TunisiaDepartment of Biology, College of Sciences, University of Hail, P.O. Box 2440, Ha’il City 81451, Saudi ArabiaDepartment of Biology, College of Sciences, University of Hail, P.O. Box 2440, Ha’il City 81451, Saudi ArabiaLaboratory of Biotechnology and Plant Improvement, Center of Biotechnology of Sfax, P.O. Box 1177, Sfax 3018, TunisiaCatalase is a crucial enzyme in the antioxidant defense system protecting organisms from oxidative stress. Proteins of this kind play important roles in controlling plant response to biotic and abiotic stresses by catalyzing the decomposition of H<sub>2</sub>O<sub>2</sub>. The durum wheat catalase 1, TdCAT1, has been previously isolated and characterized. Here, using bio-informatic analysis, we showed that durum wheat catalase 1 TdCAT1 harbors different novel conserved domains. In addition, TdCAT1 contains various phosphorylation residues and S-Nitrosylation residues located at different positions along the protein sequence. TdCAT1 activity decreased after treatment with λ−phosphatase. On the other hand, we showed that durum wheat catalase 1 (TdCAT1) exhibits a low CAT activity in vitro, whereas a deleted form of TdCAT1 has better activity compared to the full-length protein (TdCAT460), suggesting that TdCAT1 could present a putative autoinhibitory domain in its C-terminal portion. Moreover, we showed that TdCAT1 positively regulates <i>E. coli</i> cells in response to salt, ionic and osmotic stresses as well as heavy metal stress in solid and liquid mediums. Such effects had not been reported and lead us to suggest that the durum wheat catalase 1 TdCAT1 protein could play a positive role in response to a wide array of abiotic stress conditions.https://www.mdpi.com/2076-3921/11/9/1820abiotic stressbioinformatic analysisdurum wheat<i>E. coli</i>growth inhibitioncatalase |
spellingShingle | Mouna Ghorbel Kaouthar Feki Sana Tounsi Nouha Bouali Malek Besbes Faiçal Brini The Putative Auto-Inhibitory Domain of Durum Wheat Catalase (TdCAT1) Positively Regulates Bacteria Cells in Response to Different Stress Conditions Antioxidants abiotic stress bioinformatic analysis durum wheat <i>E. coli</i> growth inhibition catalase |
title | The Putative Auto-Inhibitory Domain of Durum Wheat Catalase (TdCAT1) Positively Regulates Bacteria Cells in Response to Different Stress Conditions |
title_full | The Putative Auto-Inhibitory Domain of Durum Wheat Catalase (TdCAT1) Positively Regulates Bacteria Cells in Response to Different Stress Conditions |
title_fullStr | The Putative Auto-Inhibitory Domain of Durum Wheat Catalase (TdCAT1) Positively Regulates Bacteria Cells in Response to Different Stress Conditions |
title_full_unstemmed | The Putative Auto-Inhibitory Domain of Durum Wheat Catalase (TdCAT1) Positively Regulates Bacteria Cells in Response to Different Stress Conditions |
title_short | The Putative Auto-Inhibitory Domain of Durum Wheat Catalase (TdCAT1) Positively Regulates Bacteria Cells in Response to Different Stress Conditions |
title_sort | putative auto inhibitory domain of durum wheat catalase tdcat1 positively regulates bacteria cells in response to different stress conditions |
topic | abiotic stress bioinformatic analysis durum wheat <i>E. coli</i> growth inhibition catalase |
url | https://www.mdpi.com/2076-3921/11/9/1820 |
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