ArticleJournal of bacteriology2011
RcnB is a periplasmic protein essential for maintaining intracellular Ni and Co concentrations in Escherichia coli.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 60 citations in OpenAlex.
- Disruption ofVirulence · 2026Article
- De novo origin of numerous microproteins in enterobacteria.Nucleic acids research · 2025Article
- Genome-Wide Screens Identify Genes Responsible for Intrinsic Boric Acid Resistance in Escherichia coli.Biological trace element research · 2024Article
- Heavy metal resistance in the Yanomami and Tunapuco microbiome.Memorias do Instituto Oswaldo Cruz · 2023Article
- Targeting virulence regulation to disarmVirulence · 2022Article
- FLASHIda enables intelligent data acquisition for top-down proteomics to boost proteoform identification counts.Nature communications · 2022Article
- The MreA Metal-Binding Sites C40, H65, and C69 Play a Critical Role in the Metal Tolerance of Pseudomonas putida KT2440.Current microbiology · 2022Article
- Genomics and Virulence ofMicroorganisms · 2021Article
- Using a Riboswitch Sensor to Detect CoFrontiers in chemistry · 2021Article
- Pan-transcriptomic analysis identified common differentially expressed genes of Acinetobacter baumannii in response to polymyxin treatments.Molecular omics · 2020Article
- Complexation of the nickel and cobalt transcriptional regulator RcnR with DNA.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Impact of Different Trace Elements on the Growth and Proteome of Two Strains ofFrontiers in microbiology · 2020Article
- Efficient Overproduction of Active Nitrile Hydratase by Coupling Expression Induction and Enzyme MaturationFrontiers in bioengineering and biotechnology · 2020Article
- Nickel Metalloregulators and Chaperones.Inorganics · 2019Article
- Uropathogenic enterobacteria use the yersiniabactin metallophore system to acquire nickel.The Journal of biological chemistry · 2018Article
- Co(II) and Ni(II) binding of theThe Journal of biological chemistry · 2018Article
- Glutamate Ligation in the Ni(II)- and Co(II)-Responsive Escherichia coli Transcriptional Regulator, RcnR.Inorganic chemistry · 2017Article
- Pushing the limits of nickel detection to nanomolar range using a set of engineered bioluminescent Escherichia coli.Environmental science and pollution research international · 2017Article
- Systems biology perspectives on minimal and simpler cells.Microbiology and molecular biology reviews : MMBR · 2014Review
- Combined systems approaches reveal highly plastic responses to antimicrobial peptide challenge in Escherichia coli.PLoS pathogens · 2014Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nickel and cobalt are both essential trace elements that are toxic when present in excess. The main resistance mechanism that bacteria use to overcome this toxicity is the efflux of these cations out of the cytoplasm. RND (resistance-nodulation-cell division)- and MFS (major facilitator superfamily)-type efflux systems are known to export either nickel or cobalt. The RcnA efflux pump, which belongs to a unique family, is responsible for the detoxification of Ni and Co in Escherichia coli. In this work, the role of the gene yohN, which is located downstream of rcnA, is investigated. yohN is cotranscribed with rcnA, and its expression is induced by Ni and Co. Surprisingly, in contrast to the effect of deleting rcnA, deletion of yohN conferred enhanced resistance to Ni and Co in E. coli, accompanied by decreased metal accumulation. We show that YohN is localized to the periplasm and does not bind Ni or Co ions directly. Physiological and genetic experiments demonstrate that YohN is not involved in Ni import. YohN is conserved among proteobacteria and belongs to a new family of proteins; consequently, yohN has been renamed rcnB. We show that the enhanced resistance of rcnB mutants to Ni and Co and their decreased Ni and Co intracellular accumulation are linked to the greater efflux of these ions in the absence of rcnB. Taken together, these results suggest that RcnB is required to maintain metal ion homeostasis, in conjunction with the efflux pump RcnA, presumably by modulating RcnA-mediated export of Ni and Co to avoid excess efflux of Ni and Co ions via an unknown novel mechanism.
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