Evidence map›Paper›PMID 19363090›Full record

ArticlePlant physiology2009

Mitochondrial and nuclear localization of a novel pea thioredoxin: identification of its mitochondrial target proteins.

María C Martí, Enrique Olmos, Juan J Calvete, Isabel Díaz, Sergio Barranco-Medina, James Whelan, Juan J Lázaro, Francisca Sevilla, Ana Jiménez

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.5field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

36 citing papers in PubMed, 95 citations in OpenAlex.

  1. Linking redox and calcium signaling via thioredoxins.Journal of experimental botany · 2026
    Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. ThioredoxinAntioxidants (Basel, Switzerland) · 2021
    Article
  11. Decreased Levels of ThioredoxinInternational journal of molecular sciences · 2021
    Article
  12. Genome communication in plants mediated by organelle-n-ucleus-located proteins.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020
    Review
  13. Review
  14. Redox-mediated kick-start of mitochondrial energy metabolism drives resource-efficient seed germination.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Review
  16. Review
  17. Review
  18. Article
  19. Article
  20. MitochondrialAntioxidants (Basel, Switzerland) · 2018
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

María C MartíDepartment of Stress Biology and Plant Pathology, Centro de Edafología y Biología Aplicada del Segura, Consejo Superior de Investigaciones Científicas, E-30100 Murcia, Spain.
Enrique Olmos
Juan J Calvete
Isabel Díaz
Sergio Barranco-Medina
James Whelan
Juan J Lázaro
Francisca Sevilla
Ana Jiménez
Consejo Superior de Investigaciones Científicas · ESCentro de Edafología y Biología Aplicada del Segura · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plants contain several genes encoding thioredoxins (Trxs), small proteins involved in the regulation of the activity of many enzymes through dithiol-disulfide exchange. In addition to chloroplastic and cytoplasmic Trx systems, plant mitochondria contain a reduced nicotinamide adenine dinucleotide phosphate-dependent Trx reductase and a specific Trx o, and to date, there have been no reports of a gene encoding a plant nuclear Trx. We report here the presence in pea (Pisum sativum) mitochondria and nuclei of a Trx isoform (PsTrxo1) that seems to belong to the Trx o group, although it differs from this Trx type by its absence of introns in the genomic sequence. Western-blot analysis with isolated mitochondria and nuclei, immunogold labeling, and green fluorescent protein fusion constructs all indicated that PsTrxo1 is present in both cell compartments. Moreover, the identification by tandem mass spectrometry of the native mitochondrial Trx after gel filtration using the fast-protein liquid chromatography system of highly purified mitochondria and the in vitro uptake assay into isolated mitochondria also corroborated a mitochondrial location for this protein. The recombinant PsTrxo1 protein has been shown to be reduced more effectively by the Saccharomyces cerevisiae mitochondrial Trx reductase Trr2 than by the wheat (Triticum aestivum) cytoplasmic reduced nicotinamide adenine dinucleotide phosphate-dependent Trx reductase. PsTrxo1 was able to activate alternative oxidase, and it was shown to interact with a number of mitochondrial proteins, including peroxiredoxin and enzymes mainly involved in the photorespiratory process.

Indexed as

Alternative OxidaseAmino Acid SequenceBiological AssayCell NucleusCloning, MolecularGreen Fluorescent ProteinsImmunohistochemistryMitochondriaMitochondrial ProteinsMolecular Sequence DataOxidation-ReductionOxidoreductasesPisum sativumPlant LeavesPlant ProteinsProtein TransportAlternative OxidaseGreen Fluorescent ProteinsMitochondrial ProteinsOxidoreductasesPlant ProteinsRecombinant Fusion ProteinsThioredoxins

Identifiers

PMID19363090
PMCPMC2689981
OpenAlexW2125767539

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.