Evidence map›Paper›PMID 24962998›Full record

ArticleJournal of experimental botany2014

MSRB7 reverses oxidation of GSTF2/3 to confer tolerance of Arabidopsis thaliana to oxidative stress.

Shu-Hong Lee, Chia-Wen Li, Kah Wee Koh, Hsin-Yu Chuang, Yet-Ran Chen, Choun-Sea Lin, Ming-Tsair Chan

Open access · bronzeAbstract read
In one paragraph

Article in Journal of experimental botany, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

24 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
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  5. FLS2-RBOHD module regulates changes in the metabolome ofPlant-environment interactions (Hoboken, N.J.) · 2023
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  7. Article
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  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Methionine sulfoxide reductase B fromThe Journal of biological chemistry · 2020
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Feedback Microtubule Control and Microtubule-Actin Cross-talk inMolecular & cellular proteomics : MCP · 2017
    Article
  20. Review
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

7 authors at 3 institutions in 1 country.

Shu-Hong LeeInstitute of Biotechnology, National Cheng Kung University, Tainan, 701, Taiwan Academia Sinica Biotechnology Center in Southern Taiwan, Tainan, 741, Taiwan Agricultural Biotechnology Research Center, Academia Sinica, Taipei, 115, Taiwan.
Chia-Wen LiDepartment of Biotechnology, TransWorld University, Douliu City, Yunlin County, 640, Taiwan.
Kah Wee KohAcademia Sinica Biotechnology Center in Southern Taiwan, Tainan, 741, Taiwan Agricultural Biotechnology Research Center, Academia Sinica, Taipei, 115, Taiwan.
Hsin-Yu ChuangAcademia Sinica Biotechnology Center in Southern Taiwan, Tainan, 741, Taiwan Agricultural Biotechnology Research Center, Academia Sinica, Taipei, 115, Taiwan.
Yet-Ran ChenAgricultural Biotechnology Research Center, Academia Sinica, Taipei, 115, Taiwan.
Choun-Sea LinAgricultural Biotechnology Research Center, Academia Sinica, Taipei, 115, Taiwan.
Ming-Tsair ChanInstitute of Biotechnology, National Cheng Kung University, Tainan, 701, Taiwan Academia Sinica Biotechnology Center in Southern Taiwan, Tainan, 741, Taiwan Agricultural Biotechnology Research Center, Academia Sinica, Taipei, 115, Taiwan mbmtchan@gate.sinica.edu.tw.
Agricultural Biotechnology Research Center, Academia Sinica · TWAcademia Sinica · TWTransWorld University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Methionine sulfoxide reductases (MSRs) catalyse the reduction of oxidized methionine residues, thereby protecting proteins against oxidative stress. Accordingly, MSRs have been associated with stress responses, disease, and senescence in a taxonomically diverse array of organisms. However, the cytosolic substrates of MSRs in plants remain largely unknown. Here, we used a proteomic analysis strategy to identify MSRB7 substrates. We showed that two glutathione transferases (GSTs), GSTF2 and GSTF3, had fewer oxidized methionine (MetO) residues in MSRB7-overexpressing Arabidopsis thaliana plants than in wild-type plants. Conversely, GSTF2 and GSTF3 were highly oxidized and unstable in MSRB7-knockdown plants. MSRB7 was able to restore the MetO-GSTF2M100/104 and MetO-GSTF3M100 residues produced during oxidative stress. Furthermore, both GSTs were specifically induced by the oxidative stress inducer, methyl viologen. Our results indicate that specific GSTs are substrates of MSRs, which together provide a major line of defence against oxidative stress in A. thaliana.

Indexed as

Gene Expression Regulation, PlantOxidative StressAmino Acid SequenceArabidopsisArabidopsis ProteinsGlutathione TransferaseMethionine Sulfoxide ReductasesMolecular Sequence DataOxidation-ReductionReverse Transcriptase Polymerase Chain ReactionArabidopsis ProteinsGlutathione TransferaseGSTF2 protein, ArabidopsisMethionine Sulfoxide ReductasesMsrB7 protein, ArabidopsisA. thalianaglutathione transferaseLC-MS/MSmethionine sulfoxide reductase B (MSRB).methyl viologenoxidative stress

Identifiers

PMID24962998
PMCPMC4144780
OpenAlexW2147463609

What OpenQuestion holds

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LicenceCC BY
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.