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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Main Authors: Mouna Ghorbel, Kaouthar Feki, Sana Tounsi, Nouha Bouali, Malek Besbes, Faiçal Brini
Format: Article
Language:English
Published: MDPI AG 2022-09-01
Series:Antioxidants
Subjects:
Online Access:https://www.mdpi.com/2076-3921/11/9/1820
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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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