Evidence map›Paper›PMID 33531363›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Redox regulation of NADP-malate dehydrogenase is vital for land plants under fluctuating light environment.

Yuichi Yokochi, Keisuke Yoshida, Florian Hahn, Atsuko Miyagi, Ken-Ichi Wakabayashi, Maki Kawai-Yamada, Andreas P M Weber, Toru Hisabori

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.2field-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

26 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Understanding the Role of Durum Wheat ThioredoxinPlants (Basel, Switzerland) · 2026
    Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Molecular Characteristics of the Malate Dehydrogenase (MDH) Gene Family inInternational journal of molecular sciences · 2024
    Article
  10. Article
  11. Article
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  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
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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

8 authors at 3 institutions in 2 countries.

Yuichi YokochiLaboratory of Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, 226-8503 Yokohama, Japan.
Keisuke YoshidaLaboratory of Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, 226-8503 Yokohama, Japan.ORCID 0000-0001-6542-6254
Florian HahnInstitute of Plant Biochemistry, Cluster of Excellence on Plant Sciences, Center for Synthetic Life Sciences, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.ORCID 0000-0002-0215-3209
Atsuko MiyagiDepartment of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University, 338-8570 Saitama, Japan.
Ken-Ichi WakabayashiLaboratory of Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, 226-8503 Yokohama, Japan.ORCID 0000-0002-1025-9249
Maki Kawai-YamadaDepartment of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University, 338-8570 Saitama, Japan.
Andreas P M WeberInstitute of Plant Biochemistry, Cluster of Excellence on Plant Sciences, Center for Synthetic Life Sciences, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.ORCID 0000-0003-0970-4672
Toru HisaboriLaboratory of Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, 226-8503 Yokohama, Japan; thisabor@res.titech.ac.jp.ORCID 0000-0003-2046-0277
Tokyo Institute of Technology · JPCluster of Excellence on Plant Sciences · DESaitama University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many enzymes involved in photosynthesis possess highly conserved cysteine residues that serve as redox switches in chloroplasts. These redox switches function to activate or deactivate enzymes during light-dark transitions and have the function of fine-tuning their activities according to the intensity of light. Accordingly, many studies on chloroplast redox regulation have been conducted under the hypothesis that "fine regulation of the activities of these enzymes is crucial for efficient photosynthesis." However, the impact of the regulatory system on plant metabolism is still unclear. To test this hypothesis, we here studied the impact of the ablation of a redox switch in chloroplast NADP-malate dehydrogenase (MDH). By genome editing, we generated a mutant plant whose MDH lacks one of its redox switches and is active even in dark conditions. Although NADPH consumption by MDH in the dark is expected to be harmful to plant growth, the mutant line did not show any phenotypic differences under standard long-day conditions. In contrast, the mutant line showed severe growth retardation under short-day or fluctuating light conditions. These results indicate that thiol-switch redox regulation of MDH activity is crucial for maintaining NADPH homeostasis in chloroplasts under these conditions.

Indexed as

ArabidopsisArabidopsis ProteinsChloroplastsCysteineEmbryophytaLightMalate Dehydrogenase (NADP+)Oxidation-ReductionPhotosynthesisThioredoxinsArabidopsis ProteinsCysteineMalate Dehydrogenase (NADP+)Thioredoxinschloroplastgenome editingNADP-malate dehydrogenaseredox regulationthioredoxin

Identifiers

PMID33531363
PMCPMC8017969
OpenAlexW3127680339

What OpenQuestion holds

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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.