ArticleProceedings of the National Academy of Sciences of the United States of America2004
A specific form of thioredoxin h occurs in plant mitochondria and regulates the alternative oxidase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 73 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
73 citing papers in PubMed, 245 citations in OpenAlex.
- An ancient oxidase lost in vertebrates promotes extreme stress tolerance in an emerging cnidarian model for ecology, evolution and biomedicine.The Journal of experimental biology · 2026Article
- Understanding the Role of Durum Wheat ThioredoxinPlants (Basel, Switzerland) · 2026Article
- Genome-wide identification ofFrontiers in plant science · 2026Article
- Gene expression and metabolite levels converge in the thermogenic spadix of skunk cabbage.Plant physiology · 2024Article
- Article
- Reduced GSH Acts as a Metabolic Cue of OPDA Signaling in Coregulating Photosynthesis and Defense Activation under Stress.Plants (Basel, Switzerland) · 2023Article
- Mitochondria in photosynthetic cells: Coordinating redox control and energy balance.Plant physiology · 2023Article
- Thioredoxin h2 inhibits the MPKK5-MPK3 cascade to regulate the CBF-COR signaling pathway inHorticulture research · 2023Article
- Article
- Reactive oxygen species in plants: an invincible fulcrum for biotic stress mitigation.Applied microbiology and biotechnology · 2022Review
- Mitochondrial Peroxiredoxin-IIF (PRXIIF) Activity and Function during Seed Aging.Antioxidants (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
- Genome-Wide Identification and Expression Analysis of the Thioredoxin (Frontiers in genetics · 2022Article
- ThioredoxinAntioxidants (Basel, Switzerland) · 2021Article
- Decreased Levels of ThioredoxinInternational journal of molecular sciences · 2021Article
- The Complementary Roles of Chloroplast Cyclic Electron Transport and Mitochondrial Alternative Oxidase to Ensure Photosynthetic Performance.Frontiers in plant science · 2021Review
- Matrix Redox Physiology Governs the Regulation of Plant Mitochondrial Metabolism through Posttranslational Protein Modifications.The Plant cell · 2020Review
- Effects of Salicylic Acid on the Metabolism of Mitochondrial Reactive Oxygen Species in Plants.Biomolecules · 2020Review
- Thioredoxin Network in Plant Mitochondria: Cysteine S-Posttranslational Modifications and Stress Conditions.Frontiers in plant science · 2020Review
- Deficiencies in the Mitochondrial Electron Transport Chain Affect Redox Poise and Resistance TowardFrontiers in plant science · 2019Article
13 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
14 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The plant mitochondrial thioredoxin (Trx) system has been described as containing an NADPH-dependent Trx reductase and Trx o. In addition to the mitochondrial isoform, Trx o, plants are known to contain several chloroplastic Trx isoforms and the cytosolic Trx h isoforms. We report here the presence in plant mitochondria of a Trx isoform (PtTrxh2) belonging to the Trx h group. Western blot analyses with mitochondrial proteins isolated from both poplar and GFP fusion constructs indicate that PtTrxh2 is targeted to plant mitochondria. The recombinant protein, PtTrxh2, has been shown to be reduced efficiently by the mitochondrial Trx reductase AtNTRA. PtTrxh2 is also able to reduce alternative oxidase homodimers and to allow its activation by pyruvate. In contrast, neither PtTrxh2 nor AtTrxo1 exhibits activity with several poplar glutathione peroxidases and especially a putative mitochondrial isoform. Incubation of PtTrxh2 with glutathione disulfide led to the formation of glutathionylated Trx, identified by mass spectrometry. The formation of a glutathione adduct increases the redox potential of PtTrxh2 from -290 to -225 mV. In addition to Trx o, this study shows that Trx h could also be present in mitochondria. This previously unrecognized complexity is not unexpected, considering the multiple redox-regulated processes found in plant mitochondria.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.