ArticlePlant physiology2012
Atypical thioredoxins in poplar: the glutathione-dependent thioredoxin-like 2.1 supports the activity of target enzymes possessing a single redox active cysteine.
Article in Plant physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 47 citations in OpenAlex.
- Transcriptomics-proteomics analysis reveals the role of SiNRX1 in regulating drought stress in foxtail millet (Setaria italica L.).BMC genomics · 2025Article
- Plastidial thioredoxin-like proteins are essential for normal embryogenesis and seed development in Arabidopsis thaliana.Journal of plant research · 2025Article
- Dual Roles of Reducing Systems in Protein Persulfidation and Depersulfidation.Antioxidants (Basel, Switzerland) · 2025Review
- Thioredoxin h2 inhibits the MPKK5-MPK3 cascade to regulate the CBF-COR signaling pathway inHorticulture research · 2023Article
- Article
- NewAntioxidants (Basel, Switzerland) · 2022Article
- Focus on Nitric Oxide Homeostasis: Direct and Indirect Enzymatic Regulation of Protein Denitrosation Reactions in Plants.Antioxidants (Basel, Switzerland) · 2022Review
- Thiol Reductases inAntioxidants (Basel, Switzerland) · 2022Review
- Genome-wide identification, characterization, evolution, and expression pattern analyses of the typical thioredoxin gene family in wheat (Frontiers in plant science · 2022Article
- Impact of key residues within chloroplast thioredoxin-The Journal of biological chemistry · 2019Article
- New Light on Chloroplast Redox Regulation: Molecular Mechanism of Protein Thiol Oxidation.Frontiers in plant science · 2019Review
- Dark deactivation of chloroplast enzymes finally comes to light.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Thioredoxin-like2/2-Cys peroxiredoxin redox cascade supports oxidative thiol modulation in chloroplasts.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Article
- Chloroplast FBPase and SBPase are thioredoxin-linked enzymes with similar architecture but different evolutionary histories.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Dimerization and thiol sensitivity of the salicylic acid binding thimet oligopeptidases TOP1 and TOP2 define their functions in redox-sensitive cellular pathways.Frontiers in plant science · 2015Article
- Toward a refined classification of class I dithiol glutaredoxins from poplar: biochemical basis for the definition of two subclasses.Frontiers in plant science · 2013Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plant thioredoxins (Trxs) constitute a complex family of thiol oxidoreductases generally sharing a WCGPC active site sequence. Some recently identified plant Trxs (Clot, Trx-like1 and -2, Trx-lilium1, -2, and -3) display atypical active site sequences with altered residues between the two conserved cysteines. The transcript expression patterns, subcellular localizations, and biochemical properties of some representative poplar (Populus spp.) isoforms were investigated. Measurements of transcript levels for the 10 members in poplar organs indicate that most genes are constitutively expressed. Using transient expression of green fluorescent protein fusions, Clot and Trx-like1 were found to be mainly cytosolic, whereas Trx-like2.1 was located in plastids. All soluble recombinant proteins, except Clot, exhibited insulin reductase activity, although with variable efficiencies. Whereas Trx-like2.1 and Trx-lilium2.2 were efficiently regenerated both by NADPH-Trx reductase and glutathione, none of the proteins were reduced by the ferredoxin-Trx reductase. Only Trx-like2.1 supports the activity of plastidial thiol peroxidases and methionine sulfoxide reductases employing a single cysteine residue for catalysis and using a glutathione recycling system. The second active site cysteine of Trx-like2.1 is dispensable for this reaction, indicating that the protein possesses a glutaredoxin-like activity. Interestingly, the Trx-like2.1 active site replacement, from WCRKC to WCGPC, suppresses its capacity to use glutathione as a reductant but is sufficient to allow the regeneration of target proteins employing two cysteines for catalysis, indicating that the nature of the residues composing the active site sequence is crucial for substrate selectivity/recognition. This study provides another example of the cross talk existing between the glutathione/glutaredoxin and Trx-dependent pathways.
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