Evidence map›Paper›PMID 22452855›Full record

ArticlePlant physiology2012

Thioredoxin redox regulates ATPase activity of magnesium chelatase CHLI subunit and modulates redox-mediated signaling in tetrapyrrole biosynthesis and homeostasis of reactive oxygen species in pea plants.

Tao Luo, Tingting Fan, Yinan Liu, Maxi Rothbart, Jing Yu, Shuaixiang Zhou, Bernhard Grimm, Meizhong Luo

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

33 citing papers in PubMed, 95 citations in OpenAlex.

  1. Article
  2. Review
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  5. Article
  6. Article
  7. Article
  8. Decreased Levels of ThioredoxinInternational journal of molecular sciences · 2021
    Article
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  10. Article
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  15. Two distinct redox cascades cooperatively regulate chloroplast functions and sustain plant viability.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  16. Article
  17. Review
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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 1 institution in 1 country.

Tao LuoNational Key Laboratory of Crop Genetic Improvement, Huazhong Agricultural University, Wuhan 430070, People's Republic of China.
Tingting Fan
Yinan Liu
Maxi Rothbart
Jing Yu
Shuaixiang Zhou
Bernhard Grimm
Meizhong Luo
Huazhong Agricultural University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The chloroplast thioredoxins (TRXs) function as messengers of redox signals from ferredoxin to target enzymes. In this work, we studied the regulatory impact of pea (Pisum sativum) TRX-F on the magnesium (Mg) chelatase CHLI subunit and the enzymatic activation of Mg chelatase in vitro and in vivo. In vitro, reduced TRX-F activated the ATPase activity of pea CHLI and enhanced the activity of Mg chelatase reconstituted from the three recombinant subunits CHLI, CHLD, and CHLH in combination with the regulator protein GENOMES UNCOUPLED4 (GUN4). Yeast two-hybrid and bimolecular fluorescence complementation assays demonstrated that TRX-F physically interacts with CHLI but not with either of the other two subunits or GUN4. In vivo, virus-induced TRX-F gene silencing (VIGS-TRX-F) in pea plants did not result in an altered redox state of CHLI. However, simultaneous silencing of the pea TRX-F and TRX-M genes (VIGS-TRX-F/TRX-M) resulted in partially and fully oxidized CHLI in vivo. VIGS-TRX-F/TRX-M plants demonstrated a significant reduction in Mg chelatase activity and 5-aminolevulinic acid synthesizing capacity as well as reduced pigment content and lower photosynthetic capacity. These results suggest that, in vivo, TRX-M can compensate for a lack of TRX-F and that both TRXs act as important redox regulators of Mg chelatase. Furthermore, the silencing of TRX-F and TRX-M expression also affects gene expression in the tetrapyrrole biosynthesis pathway and leads to the accumulation of reactive oxygen species, which may also serve as an additional signal for the transcriptional regulation of photosynthesis-associated nuclear genes.

Indexed as

Adenosine TriphosphatasesAgrobacteriumAminolevulinic AcidCell NucleusChlorophyllChloroplast ThioredoxinsEnzyme ActivationGene SilencingGenes, PlantHomeostasisLyasesMolecular Sequence DataNicotianaOxidation-ReductionPhenotypePhotosynthesisAdenosine TriphosphatasesAminolevulinic AcidChlorophyllChloroplast ThioredoxinsLyasesmagnesium chelatasePlant ProteinsReactive Oxygen SpeciesTetrapyrroles

Identifiers

PMID22452855
PMCPMC3375955
OpenAlexW2005142351

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.