Evidence map›Paper›PMID 20040542›Full record

ArticleThe Plant cell2009

Arabidopsis Tic62 and ferredoxin-NADP(H) oxidoreductase form light-regulated complexes that are integrated into the chloroplast redox poise.

J P Benz, A Stengel, M Lintala, Y-H Lee, A Weber, K Philippar, I L Gügel, S Kaieda, T Ikegami, P Mulo and 2 more

Open access · greenAbstract read
In one paragraph

Article in The Plant cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

51 citing papers in PubMed, 116 citations in OpenAlex.

  1. Confocal Laser Scanning Microscopy of Light-Independent ROS inInternational journal of molecular sciences · 2025
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  8. Deciphering the Molecular Mechanisms of Chilling Tolerance inInternational journal of molecular sciences · 2022
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  13. Change in HPlants (Basel, Switzerland) · 2021
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  14. Article
  15. Review
  16. Article
  17. Developmental acclimation of the thylakoid proteome to light intensity in Arabidopsis.The Plant journal : for cell and molecular biology · 2021
    Article
  18. Inactivation of HPlants (Basel, Switzerland) · 2020
    Article
  19. Article
  20. 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

12 authors at 7 institutions in 3 countries.

J P BenzMunich Center for Integrated Protein Science CiPS, Ludwig-Maximilians-Universität München, D-81377 Munich, Germany.
A Stengel
M Lintala
Y-H Lee
A Weber
K Philippar
I L Gügel
S Kaieda
T Ikegami
P Mulo
J Soll
B Bölter
Center for Integrated Protein Science Munich · DEUniversity of Turku · FIHeinrich Heine University Düsseldorf · DEJapan Science and Technology Agency · JPLudwig-Maximilians-Universität München · DEOsaka University · JPProtein Research Foundation · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Translocation of nuclear-encoded preproteins across the inner envelope of chloroplasts is catalyzed by the Tic translocon, consisting of Tic110, Tic40, Tic62, Tic55, Tic32, Tic20, and Tic22. Tic62 was proposed to act as a redox sensor of the complex because of its redox-dependent shuttling between envelope and stroma and its specific interaction with the photosynthetic protein ferredoxin-NADP(H) oxidoreductase (FNR). However, the nature of this close relationship so far remained enigmatic. A putative additional localization of Tic62 at the thylakoids mandated further studies examining how this feature might be involved in the respective redox sensing pathway and the interaction with its partner protein. Therefore, both the association with FNR and the physiological role of the third, thylakoid-bound pool of Tic62 were investigated in detail. Coexpression analysis indicates that Tic62 has similar expression patterns as genes involved in photosynthetic functions and protein turnover. At the thylakoids, Tic62 and FNR form high molecular weight complexes that are not involved in photosynthetic electron transfer but are dynamically regulated by light signals and the stromal pH. Structural analyses reveal that Tic62 binds to FNR in a novel binding mode for flavoproteins, with a major contribution from hydrophobic interactions. Moreover, in absence of Tic62, membrane binding and stability of FNR are drastically reduced. We conclude that Tic62 represents a major FNR interaction partner not only at the envelope and in the stroma, but also at the thylakoids of Arabidopsis thaliana and perhaps all flowering plants. Association with Tic62 stabilizes FNR and is involved in its dynamic and light-dependent membrane tethering.

Indexed as

ArabidopsisArabidopsis ProteinsChloroplastsDNA, BacterialGene Expression Regulation, PlantGene Knockout TechniquesLightMembrane Transport ProteinsModels, MolecularMutagenesis, InsertionalMutationOligonucleotide Array Sequence AnalysisOxidation-ReductionOxidoreductasesPhotosynthesisProtein BindingArabidopsis ProteinsDNA, Bacterialferredoxin-NAD+ reductaseMembrane Transport ProteinsOxidoreductasesRNA, PlantT-DNATic62 protein, Arabidopsis

Identifiers

PMID20040542
PMCPMC2814497
OpenAlexW2133941922

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.