Evidence map›Paper›PMID 26991003›Full record

ArticleMolecular microbiology2016

Synergistic interaction of glyceraldehydes-3-phosphate dehydrogenase and ArsJ, a novel organoarsenical efflux permease, confers arsenate resistance.

Jian Chen, Masafumi Yoshinaga, Luis D Garbinski, Barry P Rosen

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
6.7field-weighted citation impact, top 3% 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

42 citing papers in PubMed, 102 citations in OpenAlex.

  1. Article
  2. Synergistic function of ars genes in arsenic detoxification and biosynthesis of organoarsenicals.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026
    Review
  3. Article
  4. Review
  5. Mechanisms of Arsenic Interaction inInternational journal of molecular sciences · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Proteomic Analysis of Arsenic Resistance during Cyanide Assimilation byInternational journal of molecular sciences · 2023
    Article
  14. Article
  15. Genome Sequence ofMicrobiology resource announcements · 2023
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Characterization of Two Highly Arsenic-Resistant Caulobacteraceae Strains ofInternational journal of molecular sciences · 2022
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 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.
Masafumi YoshinagaDepartment of Cellular Biology and Pharmacology, Herbert Wertheim College of Medicine, Florida International University, Miami, FL, 33199, USA.
Luis D GarbinskiDepartment 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.
Florida International University · US

Funding

Mechanisms of arsenical transportR37GM055425 · NIGMS · WAYNE STATE UNIVERSITY · PI ROSEN, BARRY P. · 2005 to 2014
$4.4M
Mechanisms of Arsenic Transport and BiotransformationsR01GM055425 · NIGMS · WAYNE STATE UNIVERSITY · PI ROSEN, BARRY P. · 1997 to 2019
$3.8M
NIGMS NIH HHS R01 GM055425NIGMS NIH HHS R37 GM055425
6 · The paper itself

Abstract

Microbial biotransformations are major contributors to the arsenic biogeocycle. In parallel with transformations of inorganic arsenic, organoarsenicals pathways have recently been recognized as important components of global cycling of arsenic. The well-characterized pathway of resistance to arsenate is reduction coupled to arsenite efflux. Here, we describe a new pathway of arsenate resistance involving biosynthesis and extrusion of an unusual pentavalent organoarsenical. A number of arsenic resistance (ars) operons have two genes of unknown function that are linked in these operons. One, gapdh, encodes the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase. The other, arsJ, encodes a major facilitator superfamily (MFS) protein. The two genes were cloned from the chromosome of Pseudomonas aeruginosa. When expressed together, but not alone, in Escherichia coli, gapdh and arsJ specifically conferred resistance to arsenate and decreased accumulation of As(V). Everted membrane vesicles from cells expressing arsJ accumulated As(V) in the presence of purified GAPDH, D-glceraldehylde 3-phosphate (G3P) and NAD(+) . GAPDH forms the unstable organoarsenical 1-arseno-3-phosphoglycerate (1As3PGA). We propose that ArsJ is an efflux permease that extrudes 1As3PGA from cells, where it rapidly dissociates into As(V) and 3-phosphoglycerate (3PGA), creating a novel pathway of arsenate resistance.

Indexed as

ArsenatesArsenicArsenitesArylsulfatasesBacterial ProteinsDrug ResistanceEscherichia coliGlyceraldehyde-3-Phosphate DehydrogenasesMultienzyme ComplexesOperonPhosphatesPseudomonas aeruginosaArsenatesArsenicarsenic acidarseniteArsenitesArylsulfatasesBacterial ProteinsGlyceraldehyde-3-Phosphate DehydrogenasesMultienzyme ComplexesPhosphates

Identifiers

PMID26991003
PMCPMC4992400
OpenAlexW2297295057

What OpenQuestion holds

Textmetadata
LicenceTDM
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.