ArticleNature communications2025
Molecular basis for the enzymatic inactivity of class III glutaredoxin ROXY9 on standard glutathionylated substrates.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Emerging roles of glutaredoxins in plant metabolism.Journal of experimental botany · 2026Review
- Molecular Analysis of Two CC-Type Glutaredoxins from the Model LegumeInternational journal of molecular sciences · 2026Article
- Making HEDS or tails of glutaredoxin catalysis: Direct reduction of bis(2-hydroxyethyl) disulfide as a non-glutathione disulfide substrate.Redox biology · 2026Article
- Genome-wide identification and expression analysis under selenium stress of glutaredoxin system genes in Cardamine hupingshanensis.BMC plant biology · 2026Article
- Genome-wide identification and characterization of the GRX gene family inFrontiers in plant science · 2026Article
- Redox-inactive CC-type glutaredoxins interfere with TGA transcription factor-dependent repression of target promoters in roots.The Plant cell · 2025Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Class I glutaredoxins (GRXs) are nearly ubiquitous proteins that catalyse the glutathione (GSH)-dependent reduction of mainly glutathionylated substrates. In land plants, a third class of GRXs has evolved (class III). Class III GRXs regulate the activity of TGA transcription factors through yet unexplored mechanisms. Here we show that Arabidopsis thaliana class III GRX ROXY9 is inactive as an oxidoreductase on widely used model substrates. Glutathionylation of the active site cysteine, a prerequisite for enzymatic activity, occurs only under highly oxidizing conditions established by the GSH/glutathione disulfide (GSSG) redox couple, while class I GRXs are readily glutathionylated even at very negative GSH/GSSG redox potentials. Thus, structural alterations in the GSH binding site leading to an altered GSH binding mode likely explain the enzymatic inactivity of ROXY9. This might have evolved to avoid overlapping functions with class I GRXs and raises questions of whether ROXY9 regulates TGA substrates through redox regulation.
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