Evidence map›Paper›PMID 22102279›Full record

ArticleThe Journal of biological chemistry2012

Efflux permease CgAcr3-1 of Corynebacterium glutamicum is an arsenite-specific antiporter.

Almudena F Villadangos, Hsueh-Liang Fu, Jose A Gil, Joris Messens, Barry P Rosen, Luis M Mateos

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. 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
1.6field-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

17 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
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  8. Article
  9. A Novel Mobile Element ICEFrontiers in microbiology · 2020
    Article
  10. Pathways of arsenic uptake and efflux.Environment international · 2019
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. ArsP: a methylarsenite efflux permease.Molecular microbiology · 2015
    Article
  16. Pathways of arsenic uptake and efflux.Current topics in membranes · 2012
    Article
  17. Arsenic and antimony transporters in eukaryotes.International journal of molecular sciences · 2012
    Review
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

6 authors at 4 institutions in 3 countries.

Almudena F VilladangosDepartamento de Biología Molecular, Área de Microbiología, Facultad de Biología-Ambientales, Universidad de León, 24071 León, Spain.
Hsueh-Liang FuDepartment of Biochemistry and Molecular Biology, Wayne State University School of Medicine, Detroit, Michigan 48201.
Jose A GilDepartamento de Biología Molecular, Área de Microbiología, Facultad de Biología-Ambientales, Universidad de León, 24071 León, Spain.
Joris MessensDepartment of Structural Biology, Vlaams Instituut voor Biotechnologie; Structural Biology Brussels, Vrije Universiteit Brussels, 1050 Brussels, Belgium; Brussels Center for Redox Biology, 1050 Brussels, Belgium.
Barry P RosenDepartment of Cellular Biology and Pharmacology, Herbert Wertheim College of Medicine, Florida International University, Miami, Florida 33099. Electronic address: brosen@fiu.edu.
Luis M MateosDepartamento de Biología Molecular, Área de Microbiología, Facultad de Biología-Ambientales, Universidad de León, 24071 León, Spain. Electronic address: luis.mateos@unileon.es.
Universidad de León · ESFlorida International University · USVrije Universiteit Brussel · BEWayne State 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 GM55425NIGMS NIH HHS R01 GM055425NIGMS NIH HHS R37 GM055425
6 · The paper itself

Abstract

Resistance to arsenite (As(III)) by cells is generally accomplished by arsenite efflux permeases from Acr3 or ArsB unrelated families. We analyzed the function of three Acr3 proteins from Corynebacterium glutamicum, CgAcr3-1, CgAcr3-2, and CgAcr3-3. CgAcr3-1 conferred the highest level of As(III) resistance and accumulation in vivo. CgAcr3-1 was also the most active when everted membranes vesicles from Escherichia coli or C. glutamicum mutants were assayed for efflux with different energy sources. As(III) and antimonite (Sb(III)) resistance and accumulation studies using E. coli or C. glutamicum arsenite permease mutants clearly show that CgAcr3-1 is specific for As(III). In everted membrane vesicles expressing CgAcr3-1, dissipation of either the membrane potential or the pH gradient of the proton motive force did not prevent As(III) uptake, whereas dissipation of both components eliminated uptake. Further, a mutagenesis study of CgAcr3-1 suggested that a conserved cysteine and glutamate are involved in active transport. Therefore, we propose that CgAcr3-1 is an antiporter that catalyzes arsenite-proton exchange with residues Cys129 and Glu305 involved in efflux.

Indexed as

Amino Acid SequenceAntiportersArsenitesBacterial ProteinsBiocatalysisBiological TransportCell MembraneCorynebacterium glutamicumHydrogen-Ion ConcentrationHydrophobic and Hydrophilic InteractionsMembrane PotentialsMembrane Transport ProteinsMolecular Sequence DataMutagenesis, Site-DirectedProtein Structure, TertiaryProtonsAntiportersarseniteArsenitesBacterial ProteinsMembrane Transport ProteinsProtons

Identifiers

PMID22102279
PMCPMC3249127
OpenAlexW2057259819

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.