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Open AccessArticle

Cytosolic Isocitrate Dehydrogenase from Arabidopsis thaliana Is Regulated by Glutathionylation

1
Laboratoire Génome et Développement des Plantes, Université Perpignan Via Domitia, F-66860 Perpignan, France
2
Laboratoire Génome et Développement des Plantes, CNRS, F-66860 Perpignan, France
3
Centre of Agricultural Biochemistry and Biotechnology, University of Agriculture Faisalabad, 38000 Faisalabad, Pakistan
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Laboratoire de Spectrométrie de Masse BioOrganique (LSMBO), IPHC, Université de Strasbourg, CNRS UMR 7178, 67037 Strasbourg, France
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Institute of Plant Sciences Paris Saclay IPS2, Université Paris-Sud, CNRS, INRA, Université Evry, Paris Diderot, Sorbonne Paris-Cité, Université Paris-Saclay, Bâtiment 630, 91405 Orsay, France
6
Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Gent, Belgium
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Center for Plant Systems Biology, VIB, 9052 Gent, Belgium
*
Author to whom correspondence should be addressed.
Antioxidants 2019, 8(1), 16; https://doi.org/10.3390/antiox8010016
Received: 15 November 2018 / Revised: 19 December 2018 / Accepted: 22 December 2018 / Published: 8 January 2019
(This article belongs to the Special Issue Thioredoxin and Glutaredoxin Systems)
NADP-dependent (Nicotinamide Adénine Dinucléotide Phosphate-dependent) isocitrate dehydrogenases (NADP-ICDH) are metabolic enzymes involved in 2-oxoglutarate biosynthesis, but they also supply cells with NADPH. Different NADP-ICDH genes are found in Arabidopsis among which a single gene encodes for a cytosolic ICDH (cICDH) isoform. Here, we show that cICDH is susceptible to oxidation and that several cysteine (Cys) residues are prone to S-nitrosylation upon nitrosoglutathione (GSNO) treatment. Moreover, we identified a single S-glutathionylated cysteine Cys363 by mass-spectrometry analyses. Modeling analyses suggest that Cys363 is not located in the close proximity of the cICDH active site. In addition, mutation of Cys363 consistently does not modify the activity of cICDH. However, it does affect the sensitivity of the enzyme to GSNO, indicating that S-glutathionylation of Cys363 is involved in the inhibition of cICDH activity upon GSNO treatments. We also show that glutaredoxin are able to rescue the GSNO-dependent inhibition of cICDH activity, suggesting that they act as a deglutathionylation system in vitro. The glutaredoxin system, conversely to the thioredoxin system, is able to remove S-nitrosothiol adducts from cICDH. Finally, NADP-ICDH activities were decreased both in a catalase2 mutant and in mutants affected in thiol reduction systems, suggesting a role of the thiol reduction systems to protect NADP-ICDH activities in planta. In line with our observations in Arabidopsis, we found that the human recombinant NADP-ICDH activity is also sensitive to oxidation in vitro, suggesting that this redox mechanism might be shared by other ICDH isoforms. View Full-Text
Keywords: Isocitrate dehydrogenase; glutathionylation; nitrosylation; glutaredoxin; Arabidopsis thaliana Isocitrate dehydrogenase; glutathionylation; nitrosylation; glutaredoxin; Arabidopsis thaliana
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Niazi, A.K.; Bariat, L.; Riondet, C.; Carapito, C.; Mhamdi, A.; Noctor, G.; Reichheld, J.-P. Cytosolic Isocitrate Dehydrogenase from Arabidopsis thaliana Is Regulated by Glutathionylation. Antioxidants 2019, 8, 16.

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