ArticleJournal of experimental botany2012
Chaperone-like properties of tobacco plastid thioredoxins f and m.
Article in Journal of experimental botany, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
25 citing papers in PubMed, 45 citations in OpenAlex.
- Disulphide maintenance systems and proteostasis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Review
- Review
- The Thioredoxin System of Mammalian Cells and Its Modulators.Biomedicines · 2022Review
- Back to the future: Transplanting the chloroplast TrxF-FBPase-SBPase redox system to cyanobacteria.Frontiers in plant science · 2022Article
- Deciphering the Proteotoxic Stress Responses Triggered by the Perturbed Thylakoid Proteostasis in Arabidopsis.Plants (Basel, Switzerland) · 2021Article
- The Arabidopsis Plastidial Glucose-6-Phosphate Transporter GPT1 is Dually Targeted to Peroxisomes via the Endoplasmic Reticulum.The Plant cell · 2020Article
- Functional Improvement of Human Cardiotrophin 1 Produced in Tobacco Chloroplasts by Co-expression with Plastid Thioredoxin m.Plants (Basel, Switzerland) · 2020Article
- NTRC and Thioredoxin f Overexpression Differentially Induces Starch Accumulation in Tobacco Leaves.Plants (Basel, Switzerland) · 2019Article
- Mitochondria Are Important Determinants of the Aging of Seeds.International journal of molecular sciences · 2019Review
- Chloroplast thioredoxin systems: prospects for improving photosynthesis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- GIGANTEA is a co-chaperone which facilitates maturation of ZEITLUPE in the Arabidopsis circadian clock.Nature communications · 2017Article
- Analysis of homo- and hetero-dimerization among the three 6-phosphogluconate dehydrogenase isoforms of Arabidopsis.Plant signaling & behavior · 2016Article
- Oral Delivery of Protein Drugs Bioencapsulated in Plant Cells.Molecular therapy : the journal of the American Society of Gene Therapy · 2016Review
- Functional analysis of thioredoxin from the desert lichen-forming fungus, Endocarpon pusillum Hedwig, reveals its role in stress tolerance.Scientific reports · 2016Article
- Comparative Proteomics Analysis of Phloem Exudates Collected during the Induction of Systemic Acquired Resistance.Plant physiology · 2016Article
- Nitrogen Assimilation, Abiotic Stress and Glucose 6-Phosphate Dehydrogenase: The Full Circle of Reductants.Plants (Basel, Switzerland) · 2016Review
- A novel thiol-reductase activity of Arabidopsis YUC6 confers drought tolerance independently of auxin biosynthesis.Nature communications · 2015Article
- A cytosolic thioredoxin acts as a molecular chaperone for peroxisome matrix proteins as well as antioxidant in peroxisome.Molecules and cells · 2015Article
- Thioredoxin-dependent regulatory networks in chloroplasts under fluctuating light conditions.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014Review
- Plastid thioredoxins: a "one-for-all" redox-signaling system in plants.Frontiers in plant science · 2013Review
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thioredoxins (Trxs) are ubiquitous disulphide reductases that play important roles in the redox regulation of many cellular processes. However, some redox-independent functions, such as chaperone activity, have also been attributed to Trxs in recent years. The focus of our study is on the putative chaperone function of the well-described plastid Trxs f and m. To that end, the cDNA of both Trxs, designated as NtTrxf and NtTrxm, was isolated from Nicotiana tabacum plants. It was found that bacterially expressed tobacco Trx f and Trx m, in addition to their disulphide reductase activity, possessed chaperone-like properties. In vitro, Trx f and Trx m could both facilitate the reactivation of the cysteine-free form of chemically denatured glucose-6 phosphate dehydrogenase (foldase chaperone activity) and prevent heat-induced malate dehydrogenase aggregation (holdase chaperone activity). Our results led us to infer that the disulphide reductase and foldase chaperone functions prevail when the proteins occur as monomers and the well-conserved non-active cysteine present in Trx f is critical for both functions. By contrast, the holdase chaperone activity of both Trxs depended on their oligomeric status: the proteins were functional only when they were associated with high molecular mass protein complexes. Because the oligomeric status of both Trxs was induced by salt and temperature, our data suggest that plastid Trxs could operate as molecular holdase chaperones upon oxidative stress, acting as a type of small stress protein.
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