Advanced search
1 file | 1.50 MB Add to list

Cytosolic isocitrate dehydrogenase from Arabidopsis thaliana is regulated by glutathionylation

(2019) ANTIOXIDANTS. 8(1).
Author
Organization
Abstract
NADP-dependent (Nicotinamide Adenine Dinucleotide 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.
Keywords
S-NITROSOGLUTATHIONE REDUCTASE, PROTEIN DENITROSYLATION, OXIDATIVE, STRESS, GENE-EXPRESSION, NADP, THIOREDOXIN, RESPONSES, MUTANT, NITROSYLATION, INACTIVATION, Isocitrate dehydrogenase, glutathionylation, nitrosylation, glutaredoxin, Arabidopsis thaliana

Downloads

  • antioxidants-08-00016 Niazi et al 2019.pdf
    • full text (Published version)
    • |
    • open access
    • |
    • PDF
    • |
    • 1.50 MB

Citation

Please use this url to cite or link to this publication:

MLA
Niazi, Adnan Khan, et al. “Cytosolic Isocitrate Dehydrogenase from Arabidopsis Thaliana Is Regulated by Glutathionylation.” ANTIOXIDANTS, vol. 8, no. 1, 2019, doi:10.3390/antiox8010016.
APA
Niazi, A. K., Bariat, L., Riondet, C., Carapito, C., M’Hamdi, A., Noctor, G., & Reichheld, J.-P. (2019). Cytosolic isocitrate dehydrogenase from Arabidopsis thaliana is regulated by glutathionylation. ANTIOXIDANTS, 8(1). https://doi.org/10.3390/antiox8010016
Chicago author-date
Niazi, Adnan Khan, Laetitia Bariat, Christophe Riondet, Christine Carapito, Amna M’Hamdi, Graham Noctor, and Jean-Philippe Reichheld. 2019. “Cytosolic Isocitrate Dehydrogenase from Arabidopsis Thaliana Is Regulated by Glutathionylation.” ANTIOXIDANTS 8 (1). https://doi.org/10.3390/antiox8010016.
Chicago author-date (all authors)
Niazi, Adnan Khan, Laetitia Bariat, Christophe Riondet, Christine Carapito, Amna M’Hamdi, Graham Noctor, and Jean-Philippe Reichheld. 2019. “Cytosolic Isocitrate Dehydrogenase from Arabidopsis Thaliana Is Regulated by Glutathionylation.” ANTIOXIDANTS 8 (1). doi:10.3390/antiox8010016.
Vancouver
1.
Niazi AK, Bariat L, Riondet C, Carapito C, M’Hamdi A, Noctor G, et al. Cytosolic isocitrate dehydrogenase from Arabidopsis thaliana is regulated by glutathionylation. ANTIOXIDANTS. 2019;8(1).
IEEE
[1]
A. K. Niazi et al., “Cytosolic isocitrate dehydrogenase from Arabidopsis thaliana is regulated by glutathionylation,” ANTIOXIDANTS, vol. 8, no. 1, 2019.
@article{8675305,
  abstract     = {NADP-dependent (Nicotinamide Adenine Dinucleotide 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.},
  articleno    = {16},
  author       = {Niazi, Adnan Khan and Bariat, Laetitia and Riondet, Christophe and Carapito, Christine and M'Hamdi, Amna and Noctor, Graham and Reichheld, Jean-Philippe},
  issn         = {2076-3921},
  journal      = {ANTIOXIDANTS},
  keywords     = {S-NITROSOGLUTATHIONE REDUCTASE,PROTEIN DENITROSYLATION,OXIDATIVE,STRESS,GENE-EXPRESSION,NADP,THIOREDOXIN,RESPONSES,MUTANT,NITROSYLATION,INACTIVATION,Isocitrate dehydrogenase,glutathionylation,nitrosylation,glutaredoxin,Arabidopsis thaliana},
  language     = {eng},
  number       = {1},
  pages        = {17},
  title        = {Cytosolic isocitrate dehydrogenase from Arabidopsis thaliana is regulated by glutathionylation},
  url          = {http://dx.doi.org/10.3390/antiox8010016},
  volume       = {8},
  year         = {2019},
}

Altmetric
View in Altmetric
Web of Science
Times cited: