Evidence map›Paper›PMID 25107975›Full record

ArticleApplied and environmental microbiology2014

An ArsR/SmtB family member is involved in the regulation by arsenic of the arsenite oxidase operon in Thiomonas arsenitoxydans.

Danielle Moinier, Djamila Slyemi, Deborah Byrne, Sabrina Lignon, Régine Lebrun, Emmanuel Talla, Violaine Bonnefoy

Open access · bronzeAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.7field-weighted citation impact, top 8% 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

15 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Structural and functional mapping ofComputational and structural biotechnology journal · 2023
    Article
  4. Article
  5. An ArsR Transcriptional Regulator FacilitatesInternational journal of molecular sciences · 2021
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Arsenite oxidase also functions as an antimonite oxidase.Applied and environmental microbiology · 2015
    Article
  15. 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 3 institutions in 1 country.

Danielle MoinierAix-Marseille Université, CNRS, Laboratoire de Chimie Bactérienne UMR7283, Marseille, France.
Djamila SlyemiAix-Marseille Université, CNRS, Laboratoire de Chimie Bactérienne UMR7283, Marseille, France.
Deborah ByrneAix-Marseille Université, CNRS, Plateforme Protéine Production et Criblage FR3479, Marseille, France.
Sabrina LignonAix-Marseille Université, CNRS, Plateforme Protéomique FR3479, Marseille, France.
Régine LebrunAix-Marseille Université, CNRS, Plateforme Protéomique FR3479, Marseille, France.
Emmanuel TallaAix-Marseille Université, CNRS, Laboratoire de Chimie Bactérienne UMR7283, Marseille, France.
Violaine BonnefoyAix-Marseille Université, CNRS, Laboratoire de Chimie Bactérienne UMR7283, Marseille, France bonnefoy@imm.cnrs.fr.
Aix-Marseille Université · FRCentre National de la Recherche Scientifique · FRBioénergétique et Ingénierie des Protéines · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The genetic organization of the aioBA operon, encoding the arsenite oxidase of the moderately acidophilic and facultative chemoautotrophic bacterium Thiomonas arsenitoxydans, is different from that of the aioBA operon in the other arsenite oxidizers, in that it encodes AioF, a metalloprotein belonging to the ArsR/SmtB family. AioF is stabilized by arsenite, arsenate, or antimonite but not molybdate. Arsenic is tightly attached to AioF, likely by cysteine residues. When loaded with arsenite or arsenate, AioF is able to bind specifically to the regulatory region of the aio operon at two distinct positions. In Thiomonas arsenitoxydans, the promoters of aioX and aioB are convergent, suggesting that transcriptional interference occurs. These results indicate that the regulation of the aioBA operon is more complex in Thiomonas arsenitoxydans than in the other aioBA containing arsenite oxidizers and that the arsenic binding protein AioF is involved in this regulation. On the basis of these data, a model to explain the tight control of aioBA expression by arsenic in Thiomonas arsenitoxydans is proposed.

Indexed as

OperonAmino Acid SequenceAntimonyArsenatesArsenicArsenitesBacterial ProteinsBetaproteobacteriaBinding SitesCysteineGene Expression Regulation, BacterialMolecular Sequence DataMolybdenumOxidoreductasesPromoter Regions, GeneticRecombinant ProteinsantimoniteAntimonyArsenatesArsenicarsenite oxidaseArsenitesBacterial ProteinsCysteineMolybdenumOxidoreductasesRecombinant Proteins

Identifiers

PMID25107975
PMCPMC4178639
OpenAlexW2122318979

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.