Evidence map›Paper›PMID 28861914›Full record

ArticleMolecular microbiology2017

A novel MAs(III)-selective ArsR transcriptional repressor.

Jian Chen, Venkadesh Sarkarai Nadar, Barry P Rosen

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

27 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Mechanisms of Arsenic Interaction inInternational journal of molecular sciences · 2025
    Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. An InducibleViruses · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. An ArsR Transcriptional Regulator FacilitatesInternational journal of molecular sciences · 2021
    Article
  17. Review
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Jian ChenDepartment of Cellular Biology and Pharmacology, Herbert Wertheim College of Medicine, Florida International University, Miami, FL 33199, USA.
Venkadesh Sarkarai NadarDepartment of Cellular Biology and Pharmacology, Herbert Wertheim College of Medicine, Florida International University, Miami, FL 33199, USA.
Barry P RosenDepartment of Cellular Biology and Pharmacology, Herbert Wertheim College of Medicine, Florida International University, Miami, FL 33199, USA.ORCID http://orcid.org/0000-0002-5230-4271
Florida International University · US

Funding

Mechanisms of Arsenic Transport and BiotransformationsR01GM055425 · NIGMS · WAYNE STATE UNIVERSITY · PI ROSEN, BARRY P. · 1997 to 2019
$3.8M
SUBSTRATE RECOGNITION IN MULTIDRUG RESISTANCER01GM052216 · NIGMS · WAYNE STATE UNIVERSITY · PI ROSEN, BARRY P. · 1995 to 2008
$1.8M
NIGMS NIH HHS R01 GM052216NIGMS NIH HHS R01 GM055425
6 · The paper itself

Abstract

Microbial expression of genes for resistance to heavy metals and metalloids is usually transcriptionally regulated by the toxic ions themselves. Arsenic is a ubiquitous, naturally occurring toxic metalloid widely distributed in soil and groundwater. Microbes biotransform both arsenate (As(V)) and arsenite (As(III)) into more toxic methylated metabolites methylarsenite (MAs(III)) and dimethylarsenite (DMAs(III)). Environmental arsenic is sensed by members of the ArsR/SmtB family. The arsR gene is autoregulated and is typically part of an operon that contains other ars genes involved in arsenic detoxification. To date every identified ArsR is regulated by inorganic As(III). Here we described a novel ArsR from Shewanella putrefaciens selective for MAs(III). SpArsR orthologs control expression of two MAs(III) resistance genes, arsP that encodes the ArsP MAs(III) efflux permease, and arsH encoding the ArsH MAs(III) oxidase. SpArsR has two conserved cysteine residues, Cys101 and Cys102. Mutation of either resulted in loss of MAs(III) binding, indicating that they form an MAs(III) binding site. SpArsR can be converted into an As(III)-responsive repressor by introduction of an additional cysteine that allows for three-coordinate As(III) binding. Our results indicate that SpArsR evolved selectivity for MAs(III) over As(III) in order to control expression of genes for MAs(III) detoxification.

Indexed as

Amino Acid SequenceAnti-Bacterial AgentsArsenatesArsenicArsenicalsArsenitesBacterial ProteinsBinding SitesBiotransformationCacodylic AcidGene Expression Regulation, BacterialMembrane Transport ProteinsOperonRepressor ProteinsShewanella putrefaciensAnti-Bacterial AgentsArsenatesArsenicarsenic acidArsenicalsarseniteArsenitesBacterial ProteinsCacodylic AcidMembrane Transport ProteinsmethylarsoniteRepressor Proteins

Identifiers

PMID28861914
PMCPMC5653410
OpenAlexW2753509006

What OpenQuestion holds

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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.