Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The cobalt, zinc, and cadmium efflux system CzcABC from Alcaligenes eutrophus functions as a cation-proton antiporter in Escherichia coli.

Journal of bacteriology - 1 May 1995

Nies D H

Abstract excerpt

The function of the CzcABC protein complex, which mediates resistance to Co2+, Zn2+, and Cd2+ in Alcaligenes eutrophus by cation efflux, was investigated by using everted membrane vesicles of Escherichia coli and an acridine orange fluorescence quenching assay. Since metal cation uptake could not be measured with inside-out membrane vesicles prepared from A. eutrophus and since available E. coli strains did not...

Topics

Alcaligenes
Antiporters
Biological Transport
Cadmium
Cations
Cell Polarity
Cobalt
Drug Resistance, Microbial
Escherichia coli
Membranes
Mutation
Protons

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Zinc

Source

Open in PubMed Open full text

Identifiers

PMID: 7751279
DOI: 10.1128/jb.177.10.2707-2712.1995
PMCID: PMC176940

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7751279-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The cobalt, zinc, and cadmium efflux system CzcABC from Alcaligenes eutrophus functions as a cation-proton antiporter in Escherichia coli.PMID 7751279Read ↗

Envelope destabilization by AcrAB2NodT overexpression links antibiotic resistance to metal sensitivity in Caulobacter vibrioides.Semantic proximity Read ↗

The molecular basis of <i>Acinetobacter baumannii</i> cadmium toxicity and resistanceSemantic proximity Read ↗

CzcR-CzcS, a two-component system involved in heavy metal and carbapenem resistance in Pseudomonas aeruginosa.Semantic proximity Read ↗

A new type of Alcaligenes eutrophus CH34 zinc resistance generated by mutations affecting regulation of the cnr cobalt-nickel resistance system.Semantic proximity Read ↗

A study on the dynamics of the zraP gene expression profile and its application to the construction of zinc adsorption bacteria.Semantic proximity Read ↗

The Role of CzcRS Two-Component Systems in the Heavy Metal Resistance of Pseudomonas putida X4.Semantic proximity Read ↗

Two types of Bacillus subtilis tetA(L) deletion strains reveal the physiological importance of TetA(L) in K(+) acquisition as well as in Na(+), alkali, and tetracycline resistance.Semantic proximity Read ↗

Comparative Phenotypic Analysis of Anabaena sp. PCC 7120 Mutants of Porinlike Genes.Semantic proximity Read ↗

Zinc(II) tolerance in Escherichia coli K-12: evidence that the zntA gene (o732) encodes a cation transport ATPase.Semantic proximity Read ↗

The transcriptional regulator CzcR modulates antibiotic resistance and quorum sensing in Pseudomonas aeruginosa.Semantic proximity Read ↗

Metal Selectivity of a Cd-, Co-, and Zn-Transporting P1B-type ATPase.Semantic proximity Read ↗

A Zn(II)-translocating P-type ATPase from Proteus mirabilis.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.