Evidence map›Paper›PMID 20947511›Full record

ArticleThe Journal of biological chemistry2010

Novel channel enzyme fusion proteins confer arsenate resistance.

Binghua Wu, Jie Song, Eric Beitz

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.5field-weighted citation impact, top 9% 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

18 citing papers in PubMed, 50 citations in OpenAlex.

  1. 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
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  15. Aquaglyceroporins: generalized metalloid channels.Biochimica et biophysica acta · 2014
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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.

Binghua WuDepartment of Pharmaceutical and Medicinal Chemistry, Christian-Albrechts-Universität zu Kiel, 24118 Kiel, Germany.
Jie Song
Eric Beitz
Kiel University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Steady exposure to environmental arsenic has led to the evolution of vital cellular detoxification mechanisms. Under aerobic conditions, a two-step process appears most common among microorganisms involving reduction of predominant, oxidized arsenate (H(2)As(V)O(4)(-)/HAs(V)O(4)(2-)) to arsenite (As(III)(OH)(3)) by a cytosolic enzyme (ArsC; Escherichia coli type arsenate reductase) and subsequent extrusion via ArsB (E. coli type arsenite transporter)/ACR3 (yeast type arsenite transporter). Here, we describe novel fusion proteins consisting of an aquaglyceroporin-derived arsenite channel with a C-terminal arsenate reductase domain of phosphotyrosine-phosphatase origin, providing transposable, single gene-encoded arsenate resistance. The fusion occurred in actinobacteria from soil, Frankia alni, and marine environments, Salinispora tropica; Mycobacterium tuberculosis encodes an analogous ACR3-ArsC fusion. Mutations rendered the aquaglyceroporin channel more polar resulting in lower glycerol permeability and enhanced arsenite selectivity. The arsenate reductase domain couples to thioredoxin and can complement arsenate-sensitive yeast strains. A second isoform with a nonfunctional channel may use the mycothiol/mycoredoxin cofactor pool. These channel enzymes constitute prototypes of a novel concept in metabolism in which a substrate is generated and compartmentalized by the same molecule. Immediate diffusion maintains the dynamic equilibrium and prevents toxic accumulation of metabolites in an energy-saving fashion.

Indexed as

AquaglyceroporinsArsenatesBacteriaDrug Resistance, BacterialEscherichia coli ProteinsIon PumpsMembrane Transport ProteinsMultienzyme ComplexesRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTeratogensACR3 protein, S cerevisiaeAquaglyceroporinsArsAB ATPase, E ColiArsenatesarsenic acidEscherichia coli ProteinsIon PumpsMembrane Transport ProteinsMultienzyme ComplexesRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsTeratogens

Identifiers

PMID20947511
PMCPMC3000990
OpenAlexW1978249133

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.