Plant thioredoxins are key actors in the oxidative stress response

Santos, Christina Vieira Dos; Rey, Pascal

doi:10.1016/j.tplants.2006.05.005

Cited by 303 publications

(176 citation statements)

References 63 publications

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“…This function was clearly demonstrated by genetic means for some chloroplast thioredoxins (Vieira Dos Santos and Rey, 2006). An antioxidant function of the NTS is suggested even in the cytosol and mitochondria by the presence of the misnamed plant glutathione peroxidases (GPXs), which are in fact thioredoxin-dependent peroxidases (Iqbal et al, 2006;Navrot et al, 2006), and of peroxiredoxins (PRXs), some reducible by thioredoxins (Brehelin et al, 2003) and others by glutaredoxins (Dietz, 2003).…”

Section: The Ntra Ntrb Mutant Is Not Hypersensitive To Oxidantsmentioning

confidence: 87%

Inactivation of Thioredoxin Reductases Reveals a Complex Interplay between Thioredoxin and Glutathione Pathways in Arabidopsis Development

et al. 2007

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NADPH-dependent thioredoxin reductases (NTRs) are key regulatory enzymes determining the redox state of the thioredoxin system. The Arabidopsis thaliana genome has two genes coding for NTRs (NTRA and NTRB), both of which encode mitochondrial and cytosolic isoforms. Surprisingly, plants of the ntra ntrb knockout mutant are viable and fertile, although with a wrinkled seed phenotype, slower plant growth, and pollen with reduced fitness. Thus, in contrast with mammals, our data demonstrate that neither cytosolic nor mitochondrial NTRs are essential in plants. Nevertheless, in the double mutant, the cytosolic thioredoxin h3 is only partially oxidized, suggesting an alternative mechanism for thioredoxin reduction. Plant growth in ntra ntrb plants is hypersensitive to buthionine sulfoximine (BSO), a specific inhibitor of glutathione biosynthesis, and thioredoxin h3 is totally oxidized under this treatment. Interestingly, this BSO-mediated growth arrest is fully reversible, suggesting that BSO induces a growth arrest signal but not a toxic accumulation of activated oxygen species. Moreover, crossing ntra ntrb with rootmeristemless1, a mutant blocked in root growth due to strongly reduced glutathione synthesis, led to complete inhibition of both shoot and root growth, indicating that either the NTR or the glutathione pathway is required for postembryonic activity in the apical meristem.

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Section: The Ntra Ntrb Mutant Is Not Hypersensitive To Oxidantsmentioning

confidence: 87%

Inactivation of Thioredoxin Reductases Reveals a Complex Interplay between Thioredoxin and Glutathione Pathways in Arabidopsis Development

et al. 2007

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“…A knockout line of cytosolic GAPDH shows reduced levels of oxygen uptake and ATP but increased ROS accumulation and also a higher density of trichomes (Rius et al, 2006). TRX is a key modulator of redox status (Vieira Dos Santos and Rey, 2006). During nitrosative stress, S-nitrosylation of TRX, presumed to be S-nitrosylated at Cys-32 or Cys-35 within the active site, promotes apoptosis, presumably by inhibiting the oxidoreductase function of this enzyme and by facilitating the release of sequestered ASK1 (Sumbayev, 2003;Hess et al, 2005).…”

Section: Discussionmentioning

confidence: 99%

Nitric Oxide and ProteinS-Nitrosylation Are Integral to Hydrogen Peroxide-Induced Leaf Cell Death in Rice

et al. 2011

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Nitric oxide (NO) is a key redox-active, small molecule involved in various aspects of plant growth and development. Here, we report the identification of an NO accumulation mutant, nitric oxide excess1 (noe1), in rice (Oryza sativa), the isolation of the corresponding gene, and the analysis of its role in NO-mediated leaf cell death. Map-based cloning revealed that NOE1 encoded a rice catalase, OsCATC. Furthermore, noe1 resulted in an increase of hydrogen peroxide (H 2 O 2 ) in the leaves, which consequently promoted NO production via the activation of nitrate reductase. The removal of excess NO reduced cell death in both leaves and suspension cultures derived from noe1 plants, implicating NO as an important endogenous mediator of H 2 O 2 -induced leaf cell death. Reduction of intracellular S-nitrosothiol (SNO) levels, generated by overexpression of rice S-nitrosoglutathione reductase gene (GSNOR1), which regulates global levels of protein S-nitrosylation, alleviated leaf cell death in noe1 plants. Thus, S-nitrosylation was also involved in light-dependent leaf cell death in noe1. Utilizing the biotin-switch assay, nanoliquid chromatography, and tandem mass spectrometry, S-nitrosylated proteins were identified in both wild-type and noe1 plants. NO targets identified only in noe1 plants included glyceraldehyde 3-phosphate dehydrogenase and thioredoxin, which have been reported to be involved in S-nitrosylation-regulated cell death in animals. Collectively, our data suggest that both NO and SNOs are important mediators in the process of H 2 O 2 -induced leaf cell death in rice.

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“…ubiquitous protein-disulfide reductases that supply the reducing power needed to break disulfide bonds in physiological partners (1,2). Grxs, generally reduced by glutathione, are able to reduce protein disulfides and also to carry out the reduction of glutathione-mixed disulfides, a reaction termed deglutathionylation, for which Trxs are not efficient catalysts (3)(4)(5).…”

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confidence: 99%

Plant Thioredoxin CDSP32 Regenerates 1-Cys Methionine Sulfoxide Reductase B Activity through the Direct Reduction of Sulfenic Acid

Tarrago

Laugier²,

Zaffagnini³

et al. 2010

Journal of Biological Chemistry

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Protein electrophoresis analyses coupled to mass spectrometry revealed that CDSP32 forms a heterodimeric complex with MSRB1 via reduction of the sulfenic acid formed on MSRB1 catalytic Cys after MetSO reduction. MSR activity assays using variable CDSP32 amounts revealed that MSRB1 reduction proceeds with a 1:1 stoichiometry, and redox titrations indicated that CDSP32 and MSRB1 possess midpoints potentials of ؊337 and ؊328 mV at pH 7.9, respectively, indicating that regeneration of MSRB1 activity by the Trx through sulfenic acid reduction is thermodynamically feasible in physiological conditions.

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Plant thioredoxins are key actors in the oxidative stress response

Cited by 303 publications

References 63 publications

Inactivation of Thioredoxin Reductases Reveals a Complex Interplay between Thioredoxin and Glutathione Pathways in Arabidopsis Development

Inactivation of Thioredoxin Reductases Reveals a Complex Interplay between Thioredoxin and Glutathione Pathways in Arabidopsis Development

Nitric Oxide and ProteinS-Nitrosylation Are Integral to Hydrogen Peroxide-Induced Leaf Cell Death in Rice

Plant Thioredoxin CDSP32 Regenerates 1-Cys Methionine Sulfoxide Reductase B Activity through the Direct Reduction of Sulfenic Acid

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