ArticleProceedings of the National Academy of Sciences of the United States of America2005
Glutathionylation of chloroplast thioredoxin f is a redox signaling mechanism in plants.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
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Who cites it
66 citing papers in PubMed, 205 citations in OpenAlex.
- Emerging roles of glutaredoxins in plant metabolism.Journal of experimental botany · 2026Review
- Comprehensive identification of glutathione peroxidase (GPX) gene family and effect of GhGPX4 on reactive oxygen species metabolism in cotton.Frontiers in plant science · 2026Article
- Plastidial phosphoglucose isomerase undergoes thioredoxin-mediated redox modification without altering catalytic activity.The Biochemical journal · 2025Article
- Regulatory Effects of Different Doses of Penoxsulam on Endogenous Hormones and Antioxidant System in Foxtail Millet.Plants (Basel, Switzerland) · 2025Article
- Glutathionylation-mediated degradation of a cap-binding protein enhances Arabidopsis resistance to Plutella xylostella.The Plant cell · 2025Article
- Chloroplasts lacking class I glutaredoxins are functional but show a delayed recovery of protein cysteinyl redox state after oxidative challenge.Redox biology · 2024Article
- Fine mapping and candidate gene analysis of qSB12TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2023Article
- Current Insights into the Redox Regulation Network in Plant Chloroplasts.Plant & cell physiology · 2023Review
- Biological Functions of Hydrogen Sulfide in Plants.International journal of molecular sciences · 2022Review
- Reactive oxygen species in plants: an invincible fulcrum for biotic stress mitigation.Applied microbiology and biotechnology · 2022Review
- Adenylates regulate Arabidopsis plastidial thioredoxin activities through the binding of a CBS domain protein.Plant physiology · 2022Article
- Focus on Nitric Oxide Homeostasis: Direct and Indirect Enzymatic Regulation of Protein Denitrosation Reactions in Plants.Antioxidants (Basel, Switzerland) · 2022Review
- Plasticity in plastid redox networks: evolution of glutathione-dependent redox cascades and glutathionylation sites.BMC plant biology · 2021Article
- Selective redox signaling shapes plant-pathogen interactions.Plant physiology · 2021Review
- Atypical Iron-Sulfur Cluster Binding, Redox Activity and Structural Properties ofAntioxidants (Basel, Switzerland) · 2021Article
- ThioredoxinAntioxidants (Basel, Switzerland) · 2021Article
- Crosstalk between Brassinosteroid and Redox Signaling Contributes to the Activation of CBF Expression during Cold Responses in Tomato.Antioxidants (Basel, Switzerland) · 2021Article
- The In Vitro Interaction of 12-Oxophytodienoic Acid and Related Conjugated Carbonyl Compounds with Thiol Antioxidants.Biomolecules · 2021Article
- Function and Regulation of Chloroplast Peroxiredoxin IIE.Antioxidants (Basel, Switzerland) · 2021Article
- Turning the Knobs: The Impact of Post-translational Modifications on Carbon Metabolism.Frontiers in plant science · 2021Review
6 more citing papers are in PubMed but not listed here.
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Authors and funding
11 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thioredoxin f (TRXf) is a key factor in the redox regulation of chloroplastic carbon fixation enzymes, whereas glutathione is an important thiol buffer whose status is modulated by stress conditions. Here, we report specific glutathionylation of TRXf. A conserved cysteine is present in the TRXf primary sequence, in addition to its two active-site cysteines. The additional cysteine becomes glutathionylated when TRXf is exposed to oxidized glutathione or to reduced glutathione plus oxidants. No other chloroplastic TRX, from either Arabidopsis or Chlamydomonas, is glutathionylated under these conditions. Glutathionylation decreases the ability of TRXf to be reduced by ferredoxin-thioredoxin reductase and results in impaired light activation of target enzymes in a reconstituted thylakoid system. Although several mammalian proteins undergoing glutathionylation have already been identified, TRXf is among the first plant proteins found to undergo this posttranslational modification. This report suggests that a crosstalk between the TRX and glutathione systems mediates a previously uncharacterized form of redox signaling in plants in stress conditions.
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