RstA-Promoted Expression of the Ferrous Iron Transporter FeoB under Iron-Replete Conditions Enhances Fur Activity in
            <i>Salmonella enterica</i>

Jeon, Ji-Hye; Kim, Hyunkeun; Yun, Jae Moon; Ryu, Sangryeol; Groisman, Eduardo A.; Shin, Dongwoo

doi:10.1128/jb.00903-08

Cited by 47 publications

(57 citation statements)

References 36 publications

(54 reference statements)

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“…The Fur protein was shown to repress feoB transcription under iron-replete conditions (3,11), while the activator Fnr protein promotes feoB transcription under anaerobic conditions (3). In the present study, we report that the FeoC protein is another factor that determines cellular levels of the FeoB Fe(II) transporter in Salmonella enterica.…”

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confidence: 64%

The FeoC Protein Leads to High Cellular Levels of the Fe(II) Transporter FeoB by Preventing FtsH Protease Regulation of FeoB in Salmonella enterica

2013

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In the gammaproteobacteria, the FeoA, FeoB, and FeoC proteins constitute the Feo system, which mediates ferrous iron [Fe(II)] import. Of these Feo proteins, FeoB is an inner membrane Fe(II) transporter that is aided by the small protein FeoA. However, the role of another small protein, FeoC, has remained unknown. Here we report that the FeoC protein is necessary for FeoB protein-mediated Fe(II) uptake in Salmonella experiencing low levels of oxygen and iron. The FeoC protein was found to directly bind to the FeoB transporter, leading to high cellular levels of FeoB. Depletion of the FtsH protease enabled high levels of FeoB in the absence of FeoC, suggesting that the FeoC protein protects the FeoB transporter from FtsH-mediated proteolysis. Our present study provides a singular example of bacteria that can control expression of iron uptake systems posttranslationally by employing a small iron transporter-binding protein.

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The FeoC Protein Leads to High Cellular Levels of the Fe(II) Transporter FeoB by Preventing FtsH Protease Regulation of FeoB in Salmonella enterica

2013

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“…Fur and Fnr play a crucial role in maintaining cellular iron homeostasis and preventing the formation of damaging free radicals. The presence of another regulatory element, the rstA box, has also been found in the Salmonella enterica feo operon, which is absent in its E. coli counterpart, to precede the fur binding sequence (24). RstA was shown to regulate the expression of the feoB gene in S. enterica (24).…”

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“…The presence of another regulatory element, the rstA box, has also been found in the Salmonella enterica feo operon, which is absent in its E. coli counterpart, to precede the fur binding sequence (24). RstA was shown to regulate the expression of the feoB gene in S. enterica (24). The Feo system is important for the virulence of various pathogenic bacterial strains such as Helicobacter pylori, Legionella pneumophila, and Campylobacter jejuni (25)(26)(27).…”

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Solution Structure of Escherichia coli FeoA and Its Potential Role in Bacterial Ferrous Iron Transport

et al. 2013

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Iron is an indispensable nutrient for most organisms. Ferric iron (Fe 3؉) predominates under aerobic conditions, while during oxygen limitation ferrous (Fe 2؉ ) iron is usually present. The Feo system is a bacterial ferrous iron transport system first discovered in Escherichia coli K-12. It consists of three genes, feoA, feoB, and feoC (yhgG). FeoB is thought to be the main transmembrane transporter while FeoC is considered to be a transcriptional regulator. Using multidimensional nuclear magnetic resonance (NMR) spectroscopy, we have determined the solution structure of E. coli FeoA. The structure of FeoA reveals a Src-homology 3 (SH3)-like fold. The structure is composed of a ␤-barrel with two ␣-helices where one helix is positioned over the barrel. In comparison to the standard eukaryotic SH3 fold, FeoA has two additional ␣-helices. FeoA was further characterized by heteronuclear NMR dynamics measurements, which suggest that it is a monomeric, stable globular protein. Model-free analysis of the NMR relaxation results indicates that a slow conformational dynamic process is occurring in ␤-strand 4 that may be important for function. 31P NMR-based GTPase activity measurements with the N-terminal domain of FeoB (NFeoB) indicate a higher GTP hydrolysis rate in the presence of potassium than with sodium. Further enzymatic assays with NFeoB suggest that FeoA may not act as a GTPase-activating protein as previously proposed. These findings, together with bioinformatics and structural analyses, suggest that FeoA may have a different role, possibly interacting with the cytoplasmic domain of the highly conserved core portion of the FeoB transmembrane region.

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“…5 Bacteria can also acquire the soluble, ferrous form of iron via the anaerobic-microaerophilic FeoAB pathway. 9 In addition, ferrous iron can be taken up by NRAMP (natural resistance-associated macrophage protein)-like transporters (e.g., MntH of E. coli), metal-type ABC transporters (e.g., SitABCD of Salmonella) and ZIP transporters (e.g., ZupT of E. coli). 10 The acquisition of iron from host proteins has been studied in just a handful of Gram-positive microbes.…”

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Identification of iron-regulated genes of Bifidobacterium breve UCC2003 as a basis for controlled gene expression

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Zomer²,

Fitzgerald³

et al. 2012

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RstA-Promoted Expression of the Ferrous Iron Transporter FeoB under Iron-Replete Conditions Enhances Fur Activity in Salmonella enterica

Abstract: The Fur protein is a primary regulator that monitors and controls cytoplasmic iron levels. We now report the identification of a regulatory pathway mediated by the Salmonella response regulator RstA that promotes

Cited by 47 publications

References 36 publications

The FeoC Protein Leads to High Cellular Levels of the Fe(II) Transporter FeoB by Preventing FtsH Protease Regulation of FeoB in Salmonella enterica

The FeoC Protein Leads to High Cellular Levels of the Fe(II) Transporter FeoB by Preventing FtsH Protease Regulation of FeoB in Salmonella enterica

Solution Structure of Escherichia coli FeoA and Its Potential Role in Bacterial Ferrous Iron Transport

Identification of iron-regulated genes of Bifidobacterium breve UCC2003 as a basis for controlled gene expression

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