Evidence map›Paper›PMID 25933432›Full record

ArticlePloS one2015

A 1-Cys Peroxiredoxin from a Thermophilic Archaeon Moonlights as a Molecular Chaperone to Protect Protein and DNA against Stress-Induced Damage.

Sangmin Lee, Baolei Jia, Jinliang Liu, Bang Phuong Pham, Jae Myeong Kwak, Yuan Hu Xuan, Gang-Won Cheong

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 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

12 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Redox and Thiols in Archaea.Antioxidants (Basel, Switzerland) · 2020
    Review
  6. Review
  7. Structure of the Prx6-subfamily 1-Cys peroxiredoxin from Sulfolobus islandicus.Acta crystallographica. Section F, Structural biology communications · 2019
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. 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

7 authors at 5 institutions in 2 countries.

Sangmin LeeDivision of Applied Life Sciences and Research Institute of Natural Science, Gyeongsang National University, Jinju, Korea; Division of Electron Microscopic Research, Korea Basic Science Institute, Daejeon, Korea.
Baolei JiaDivision of Applied Life Sciences and Research Institute of Natural Science, Gyeongsang National University, Jinju, Korea; Department of Life Sciences, Chung-Ang University, Seoul, Korea.
Jinliang LiuCollege of Plant Sciences, Jilin University, Changchun, China.
Bang Phuong PhamDivision of Applied Life Sciences and Research Institute of Natural Science, Gyeongsang National University, Jinju, Korea.
Jae Myeong KwakDivision of Applied Life Sciences and Research Institute of Natural Science, Gyeongsang National University, Jinju, Korea.
Yuan Hu XuanCollege of Pharmaceutical Sciences, Wenzhou Medical University, Wenzhou, China.
Gang-Won CheongDivision of Applied Life Sciences and Research Institute of Natural Science, Gyeongsang National University, Jinju, Korea.
Gyeongsang National University · KRChung-Ang University · KRJilin University · CNKorea Basic Science Institute · KRWenzhou Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peroxiredoxins (Prxs) act against hydrogen peroxide (H2O2), organic peroxides, and peroxynitrite. Thermococcus kodakaraensis KOD1, an anaerobic archaeon, contains many antioxidant proteins, including three Prxs (Tk0537, Tk0815, and Tk1055). Only Tk0537 has been found to be induced in response to heat, osmotic, and oxidative stress. Tk0537 was found to belong to a 1-Cys Prx6 subfamily based on sequence analysis and was named 1-Cys TkPrx. Using gel filtration chromatography, electron microscopy, and blue-native polyacrylamide gel electrophoresis, we observed that 1-Cys TkPrx exhibits oligomeric forms with reduced peroxide reductase activity as well as decameric and dodecameric forms that can act as molecular chaperones by protecting both proteins and DNA from oxidative stress. Mutational analysis showed that a cysteine residue at the N-terminus (Cys46) was responsible for the peroxide reductase activity, and cysteine residues at the C-terminus (Cys205 and Cys211) were important for oligomerization. Based on our results, we propose that interconversion between different oligomers is important for regulating the different functions of 1-Cys TkPrx.

Indexed as

DNA DamageStress, PhysiologicalArchaeal ProteinsCloning, MolecularDNA, BacterialHydroxyl RadicalMolecular ChaperonesMutant ProteinsOxidation-ReductionPeroxidasePeroxiredoxinsPoint MutationProtein BindingRecombinant ProteinsSequence Analysis, ProteinTemperatureArchaeal ProteinsDNA, BacterialHydroxyl RadicalMolecular ChaperonesMutant ProteinsPeroxidasePeroxiredoxinsRecombinant Proteins

Identifiers

PMID25933432
PMCPMC4416765
OpenAlexW2327787842

What OpenQuestion holds

Textmetadata
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.