An Atypical Catalytic Mechanism Involving Three Cysteines of Thioredoxin

Koh, Cha San; Navrot, Nicolas; Didierjean, Claude; Rouhier, Nicolas; Hirasawa, Masakazu; Knaff, David B.; Wingsle, Gunnar; Samian, Razip; Jacquot, Jean‐Pierre; Corbier, Catherine; Gelhaye, Éric

doi:10.1074/jbc.m802093200

Cited by 43 publications

(20 citation statements)

References 57 publications

(79 reference statements)

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“…6. In fact, the cross-talk between the Trx and Grx systems with the catalytic disulfide of some plant Trxs reduced by the Grx systems has been reported previously, such as poplar Trx h4 (33,34), Arabidopsis thaliana Trx h9 (35), and grape Trx h (Vitis vinifera CxxS2) (36). According to the authors, the reduction of plant Trx by the Grx system is a deglutathionylation reaction (37), which is as same as the mechanism proposed in our study.…”

Section: Discussionsupporting

confidence: 53%

Thioredoxin 1 Is Inactivated Due to Oxidation Induced by Peroxiredoxin under Oxidative Stress and Reactivated by the Glutaredoxin System

Du¹,

Zhang²,

Zhang

et al. 2013

Journal of Biological Chemistry

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Background:The Cys-62/Cys-69 dithiol of Trx1 is predicted to have a profound effect on cell signaling. Results: The Cys-62/Cys-69 dithiol of Trx1 was oxidized by Prx1, and this disulfide was reduced by the GSH/glutaredoxin system. Conclusion: Trx1 is involved in redox regulation via reversible oxidation of the Cys-62/Cys-69 dithiol of Trx1. Significance: We demonstrated the critical role of Trx1 oxidation in cell signaling.

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Section: Discussionsupporting

confidence: 53%

Thioredoxin 1 Is Inactivated Due to Oxidation Induced by Peroxiredoxin under Oxidative Stress and Reactivated by the Glutaredoxin System

Du¹,

Zhang²,

Zhang

et al. 2013

Journal of Biological Chemistry

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“…These results suggest that the TRX-mediated increase of ICL activity previously observed in total extracts of C. reinhardtii (10) was probably indirect. This apparent activation could be due to the presence of TRX-reducible GRXs in the extract (40,41) or other enzymes catalyzing deglutathionylation, such as sulfiredoxins (42,43). However, the possibility cannot be completely ruled out that a disulfide bond could be formed in CrICL in vivo under specific conditions or by interaction with partner proteins not present in our in vitro assays.…”

Section: Discussionmentioning

confidence: 77%

“…Several GRXs have been shown to be reduced by thioredoxin reductases (6,44,45). Conversely, some TRXs appear to be reduced by glutathione and/or GRX (40,41), and inactivation of NADPH-thioredoxin reductase genes in Arabidopsis revealed that an alternative reduction system allows TRX reduction in a glutathione-dependent manner, probably implicating a GRX (46). Moreover, TRXs from humans and higher plants have been shown to be regulated by glutathionylation (47)(48)(49).…”

Section: Discussionmentioning

confidence: 99%

Regulation by Glutathionylation of Isocitrate Lyase from Chlamydomonas reinhardtii

Bedhomme

Zaffagnini

Marchand

et al. 2009

Journal of Biological Chemistry

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Post-translational modification of protein cysteine residues is emerging as an important regulatory and signaling mechanism. We have identified numerous putative targets of redox regulation in the unicellular green alga Chlamydomonas reinhardtii. One enzyme, isocitrate lyase (ICL), was identified both as a putative thioredoxin target and as an S-thiolated protein in vivo. ICL is a key enzyme of the glyoxylate cycle that allows growth on acetate as a sole source of carbon. The aim of the present study was to clarify the molecular mechanism of the redox regulation of Chlamydomonas ICL using a combination of biochemical and biophysical methods. The results clearly show that purified C. reinhardtii ICL can be inactivated by glutathionylation and reactivated by glutaredoxin, whereas thioredoxin does not appear to regulate ICL activity, and no inter-or intramolecular disulfide bond could be formed under any of the conditions tested. Glutathionylation of the protein was investigated by mass spectrometry analysis, Western blotting, and site-directed mutagenesis. The enzyme was found to be protected from irreversible oxidative inactivation by glutathionylation of its catalytic Cys 178 , whereas a second residue, Cys 247 , becomes artifactually glutathionylated after prolonged incubation with GSSG. The possible functional significance of this post-translational modification of ICL in Chlamydomonas and other organisms is discussed.

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“…Indeed, in several organisms, several publications have highlighted an interplay between the NTS and NGS pathways (Carmel-Harel and Storz, 2000;Kanzok et al, 2000Kanzok et al, , 2001Gelhaye et al, 2003;Grant, 2003, 2005;Koh et al, 2008). Therefore, association of mutants involved in both the NTS and NGS pathways have recently revealed functions of these pathways in several aspects of plant development.…”

Section: Introductionmentioning

confidence: 99%

Interplay between the NADP-Linked Thioredoxin and Glutathione Systems in Arabidopsis Auxin Signaling

et al. 2010

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Intracellular redox status is a critical parameter determining plant development in response to biotic and abiotic stress. Thioredoxin (TRX) and glutathione are key regulators of redox homeostasis, and the TRX and glutathione pathways are essential for postembryonic meristematic activities. Here, we show by associating TRX reductases (ntra ntrb) and glutathione biosynthesis (cad2) mutations that these two thiol reduction pathways interfere with developmental processes through modulation of auxin signaling. The triple ntra ntrb cad2 mutant develops normally at the rosette stage, undergoes the floral transition, but produces almost naked stems, reminiscent of the phenotype of several mutants affected in auxin transport or biosynthesis. In addition, the ntra ntrb cad2 mutant shows a loss of apical dominance, vasculature defects, and reduced secondary root production, several phenotypes tightly regulated by auxin. We further show that auxin transport capacities and auxin levels are perturbed in the mutant, suggesting that the NTR-glutathione pathways alter both auxin transport and metabolism. Analysis of ntr and glutathione biosynthesis mutants suggests that glutathione homeostasis plays a major role in auxin transport as both NTR and glutathione pathways are involved in auxin homeostasis.

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An Atypical Catalytic Mechanism Involving Three Cysteines of Thioredoxin

Cited by 43 publications

References 57 publications

Thioredoxin 1 Is Inactivated Due to Oxidation Induced by Peroxiredoxin under Oxidative Stress and Reactivated by the Glutaredoxin System

Thioredoxin 1 Is Inactivated Due to Oxidation Induced by Peroxiredoxin under Oxidative Stress and Reactivated by the Glutaredoxin System

Regulation by Glutathionylation of Isocitrate Lyase from Chlamydomonas reinhardtii

Interplay between the NADP-Linked Thioredoxin and Glutathione Systems in Arabidopsis Auxin Signaling

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