ArticleJournal of bacteriology2013
FeoA and FeoC are essential components of the Vibrio cholerae ferrous iron uptake system, and FeoC interacts with FeoB.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 97 citations in OpenAlex.
- Operonic architecture of bacterial metal response: envelope constraints, evolutionary mobility, and bioremediation design rules.World journal of microbiology & biotechnology · 2026Review
- The structure of the full catalytic cycle ofbioRxiv : the preprint server for biology · 2025Article
- Characterization of intact FeoB in a lipid bilayer using styrene-maleic acid (SMA) copolymers.Biochimica et biophysica acta. Biomembranes · 2025Article
- Structural Determinants ofbioRxiv : the preprint server for biology · 2024Article
- Flipping the switch: dynamic modulation of membrane transporter activity in bacteria.Microbiology (Reading, England) · 2023Review
- The Role of Iron in Phytopathogenic Microbe-Plant Interactions: Insights into Virulence and Host Immune Response.Plants (Basel, Switzerland) · 2023Review
- Divide and conquer: genetics, mechanism, and evolution of the ferrous iron transporter Feo inFrontiers in microbiology · 2023Article
- Enterococcus faecalis thrives in dual-species biofilm models under iron-rich conditions.Archives of microbiology · 2022Article
- Enterococcus faecalis thrives in dual-species biofilm models under iron-rich conditions.Archives of microbiology · 2022Article
- A general protocol for the expression and purification of the intact transmembrane transporter FeoB.Biochimica et biophysica acta. Biomembranes · 2022Article
- The structure of Vibrio cholerae FeoC reveals conservation of the helix-turn-helix motif but not the cluster-binding domain.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Article
- The fciTABC and feoABI systems contribute to ferric citrate acquisition in Stenotrophomonas maltophilia.Journal of biomedical science · 2022Article
- Disentangling the Evolutionary History of Feo, the Major Ferrous Iron Transport System in Bacteria.mBio · 2022Article
- Iron Transport and Metabolism in Escherichia, Shigella, and Salmonella.EcoSal Plus · 2021Article
- Phenotypic and genomic characterization of aMicrobial genomics · 2021Article
- Article
- Genetic Redundancy in Iron and Manganese Transport in the Metabolically Versatile Bacterium Rhodopseudomonas palustris TIE-1.Applied and environmental microbiology · 2020Article
- Iron acquisition system of Sphingobium sp. strain SYK-6, a degrader of lignin-derived aromatic compounds.Scientific reports · 2020Article
- Iron Acquisition by Bacterial Pathogens: Beyond Tris-Catecholate Complexes.Chembiochem : a European journal of chemical biology · 2020Review
- Biochemical characterization of bacterial FeoBs: A perspective on nucleotide specificity.Archives of biochemistry and biophysics · 2020Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The ferrous iron transport system Feo is widely distributed among bacterial species, yet its physical structure and mechanism of iron transport are poorly understood. In Vibrio cholerae, the feo operon consists of three genes, feoABC. feoB encodes an 83-kDa protein with an amino-terminal GTPase domain and a carboxy-terminal domain predicted to be embedded in the inner membrane. While FeoB is believed to form the pore for iron transport, the roles of FeoA and FeoC are unknown. In this work, we show that FeoA and FeoC, as well as the more highly conserved FeoB, are all required for iron acquisition by V. cholerae Feo. An in-frame deletion of feoA, feoB, or feoC eliminated iron acquisition. The loss of transport activity in the feoA and feoC mutants was not due to reduced transcription of the feo operon, suggesting that these two small proteins are required for activity of the transporter. feoC was found to encode a protein that interacts with the cytoplasmic domain of FeoB, as determined using the BACTH bacterial two-hybrid system. Two conserved amino acids in FeoC were found to be necessary for the interaction with FeoB in the two-hybrid assay, and when either of these amino acids was mutated in the context of the entire feo operon, iron acquisition via Feo was reduced. No interaction of FeoA with FeoB or FeoC was detected in the BACTH two-hybrid assay.
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