Evidence map›Paper›PMID 25898225›Full record

ArticlePloS one2015

Three members of polyamine modulon under oxidative stress conditions: two transcription factors (SoxR and EmrR) and a glutathione synthetic enzyme (GshA).

Akihiko Sakamoto, Yusuke Terui, Taketo Yoshida, Taku Yamamoto, Hideyuki Suzuki, Kaneyoshi Yamamoto, Akira Ishihama, Kazuei Igarashi, Keiko Kashiwagi

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

17 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Evolution ofGut microbes · 2023
    Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Effects of polyamines on protein synthesis and growth ofThe Journal of biological chemistry · 2018
    Review
  11. Polyamine catabolism and oxidative damage.The Journal of biological chemistry · 2018
    Review
  12. Article
  13. Article
  14. Article
  15. Functions of Polyamines in Mammals.The Journal of biological chemistry · 2016
    Review
  16. Review
  17. 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 4 institutions in 1 country.

Akihiko SakamotoFaculty of Pharmacy, Chiba Institute of Science, Choshi, Chiba, Japan.
Yusuke TeruiFaculty of Pharmacy, Chiba Institute of Science, Choshi, Chiba, Japan.
Taketo YoshidaFaculty of Pharmacy, Chiba Institute of Science, Choshi, Chiba, Japan.
Taku YamamotoFaculty of Pharmacy, Chiba Institute of Science, Choshi, Chiba, Japan.
Hideyuki SuzukiGraduate School of Science and Technology, Kyoto Institute of Technology, Kyoto, Kyoto, Japan.
Kaneyoshi YamamotoDepartment of Frontier Bioscience, Hosei University, Koganei, Tokyo, Japan.
Akira IshihamaDepartment of Frontier Bioscience, Hosei University, Koganei, Tokyo, Japan.
Kazuei IgarashiGraduate School of Pharmaceutical Sciences, Chiba University, Chiba, Chiba, Japan; Amine Pharma Research Institute, Innovation Plaza at Chiba University, Chiba, Chiba, Japan.
Keiko KashiwagiFaculty of Pharmacy, Chiba Institute of Science, Choshi, Chiba, Japan.
Chiba Institute of Science · JPHosei University · JPAmine Pharma (Japan) · JPKyoto Institute of Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Members of polyamine modulon whose synthesis is enhanced at the level of translation were looked for under oxidative stress conditions caused by 0.6 μM K2TeO3. When an Escherichia coli polyamine-requiring mutant MA261 was cultured in the presence of K2TeO3, the degree of polyamine stimulation of cell growth was greater than in cells cultured in the absence of K2TeO3. Under these conditions, synthesis of SoxR, a transcriptional factor for expression of the superoxide response regulon, EmrR, a negative transcriptional factor for expression of the genes for drug excretion proteins, EmrA and EmrB, and of GshA, γ-glutamylcysteine synthetase necessary for glutathione (GSH) synthesis, were stimulated by polyamines at the level of translation. Polyamine stimulation of SoxR and EmrR synthesis was dependent on the existence of an unusually located Shine-Dalgarno (SD) sequence in soxR and emrR mRNAs. Polyamine stimulation of GshA synthesis was due to the existence of the inefficient initiation codon UUG instead of AUG. Polyamine stimulation of the synthesis of EmrR was mainly observed at the logarithmic phase of growth, while that of the synthesis of SoxR and GshA was at the stationary phase. These results strongly suggest that polyamines are involved in easing of oxidative stress through stimulation of synthesis of SoxR, EmrR and GshA together with RpoS, previously found as a member of polyamine modulon at the stationary phase.

Indexed as

Gene Expression Regulation, BacterialBacterial ProteinsCodon, InitiatorDipeptidesEscherichia coliEscherichia coli ProteinsGlutathioneMembrane ProteinsOxidative StressPolyaminesProtein BiosynthesisRegulonRNA, MessengerSigma FactorTranscription FactorsBacterial ProteinsCodon, InitiatorDipeptidesEmrA protein, E coliEmrB protein, E coliEscherichia coli Proteinsgamma-glutamylcysteineGlutathioneMembrane ProteinsPolyaminesRNA, MessengerSigma Factorsigma factor KatF protein, BacteriaSoxR protein, BacteriaTranscription Factors

Identifiers

PMID25898225
PMCPMC4405209
OpenAlexW2074483508

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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.