ArticleJournal of bacteriology2015
Lon-mediated proteolysis of the FeoC protein prevents Salmonella enterica from accumulating the Fe(II) transporter FeoB under high-oxygen conditions.
Article in Journal of bacteriology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 50 citations in OpenAlex.
- The dual implications of iron homeostasis as a bacterial threat: its roles in virulence and antimicrobial resistance.Archives of microbiology · 2025Review
- Lon-dependent proteolysis in oxidative stress responses.Journal of bacteriology · 2025Review
- Flipping the switch: dynamic modulation of membrane transporter activity in bacteria.Microbiology (Reading, England) · 2023Review
- Availability of Ferritin-Bound Iron to Enterobacteriaceae.International journal of molecular sciences · 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
- Dual RNA sequencing reveals dendritic cell reprogramming in response to typhoidal Salmonella invasion.Communications biology · 2022Article
- Transcriptome Analyses of Chicken Primary Macrophages Infected With AttenuatedFrontiers in microbiology · 2022Article
- Iron Transport and Metabolism in Escherichia, Shigella, and Salmonella.EcoSal Plus · 2021Article
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- Iron Limitation inFrontiers in microbiology · 2020Article
- The FeoC [4Fe-4S] Cluster Is Redox-Active and Rapidly Oxygen-Sensitive.Biochemistry · 2019Article
- A LON-ClpP Proteolytic Axis Degrades Complex I to Extinguish ROS Production in Depolarized Mitochondria.Cell reports · 2016Article
- Vibrio cholerae FeoA, FeoB, and FeoC Interact To Form a Complex.Journal of bacteriology · 2016Article
- Shigella Iron Acquisition Systems and their Regulation.Frontiers in cellular and infection microbiology · 2016Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Salmonella Feo system consists of the FeoA, FeoB, and FeoC proteins and mediates ferrous iron [Fe(II)] import. FeoB is an inner membrane protein that, along with contributions from two small hydrophilic proteins, FeoA and FeoC, transports Fe(II). We previously reported that FeoC binds to and protects the FeoB transporter from FtsH-mediated proteolysis. In the present study, we report proteolytic regulation of FeoC that occurs in an oxygen-dependent fashion. While relatively stable under low-oxygen conditions, FeoC was rapidly degraded by the Lon protease under high-oxygen conditions. The putative Fe-S cluster of FeoC seemed to function as an oxygen sensor to control FeoC stability, as evidenced by the finding that mutation of the putative Fe-S cluster-binding site greatly increased FeoC stability under high-oxygen conditions. Salmonella ectopically expressing the feoB and feoC genes was able to accumulate FeoB and FeoC only under low-oxygen conditions, suggesting that FeoC proteolysis prevents Salmonella from accumulating the FeoB transporter under high-oxygen conditions. Finally, we propose that Lon-mediated FeoC proteolysis followed by FtsH-mediated FeoB proteolysis helps Salmonella to avoid uncontrolled Fe(II) uptake during the radical environmental changes encountered when shifting from low-iron anaerobic conditions to high-iron aerobic conditions.
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