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Chapter 12 : Ferrous Iron Transport

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Ferrous Iron Transport, Page 1 of 2

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Abstract:

Transport systems for both ferric and ferrous iron have been identified in bacteria. Many bacteria produce siderophores to mobilize insoluble ferric iron from their surroundings. One of the first ferrous iron transport systems identified in bacteria, Feo, was found in . The major transport protein FeoB contains a typical nucleotide-binding motif in the first 160 N-terminal amino acid residues, and there are at least 7 carboxy-terminal α-helices that embed the protein in the cytoplasmic membrane. Although there is evidence that the transport of ferrous iron is energized by ATP hydrolysis, the nucleotide-binding motif in FeoB has more similarities to the GTP-binding sites found in Ras proteins and elongation factors than to the ATP-binding sites in bacterial ABC transporters. Although it is clear that FeoB and the associated GTPase activity are required for ferrous iron transport, the mechanism of transport and precise function of FeoB are unknown. FeoB homologs are found in genomes of archaea and gram-positive and gram-negative bacteria (COGs, or phylogenetic classification of proteins encoded in complete genomes). It has been shown that FeoB-dependent ferrous iron transport in sp. strain PCC6803 is induced under iron-limiting growth conditions. Ferrous iron uptake is also important in the presence of oxygen since many bacteria can reduce extracellular ferric iron. The striking similarity of Feo to G proteins and the wide distribution of this protein make future research on the function of this protein in ferrous iron transport an exciting task.

Citation: Hantke K. 2004. Ferrous Iron Transport, p 178-184. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch12
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Figures

Image of FIGURE 1
FIGURE 1

Schematic model of iron uptake in a gram-negative bacterium. Cells produce siderophores, which complex ferric iron. The Fe-siderophore complexes are taken up via a receptor protein, R, in the outer membrane. The uptake is dependent on the TonB complex (T). A binding protein-dependent ABC transporter allows uptake through the cytoplasmic membrane. Fe uptake through the cytoplasmic membrane may be accomplished by FeoB, possibly with the help of FeoA and FeoC, the latter being found only been found in . In oxygen-containing environments, Fe may be converted to Fe by generally uncharacterized reductive processes (“Red”) at the cell surface or in the periplasm. In gram-positive bacteria, the picture is very similar, but the outer membrane receptor (R) and the TonB complex (T) are missing.

Citation: Hantke K. 2004. Ferrous Iron Transport, p 178-184. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch12
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Image of FIGURE 2
FIGURE 2

Organization of the genes in K-12. Putative Fur- and Fnr-binding sites (not to scale) and the direction of transcription are shown.

Citation: Hantke K. 2004. Ferrous Iron Transport, p 178-184. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch12
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Image of FIGURE 3
FIGURE 3

FeoB contains a G protein. The FeoB sequences found in >95 microorganisms, including pathogenic bacteria, cyanobacteria, and archaebacteria, contain highly conserved G-protein signature motifs within domain I of NFeoB (the first 160 amino acids). While the first three consensus motifs are unambiguous, two putative copies of the fourth G-protein consensus motif (NXXD) are observed (amino acids 91 to 94 and amino acids 120 to 123 of ). Conserved amino acids are indicated by asterisks, highly similar ones are indicated by colons, and similar ones are indicated by dots.

Citation: Hantke K. 2004. Ferrous Iron Transport, p 178-184. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch12
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References

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1. Cowart, R. E. 2002. Reduction of iron by extracellular iron reductases: implications for microbial iron acquisition. Arch. Biochem. Biophys. 400:273281.
2. Hantke, K. 1987. Ferrous iron transport mutants in Escherichia coli K-12. FEMS Microbiol. Lett. 44: 5357.
3. Hantke, K. 1997. Ferrous iron uptake by a magnesium transport system is toxic for Escherichia coli and Salmonella typhimurium. J. Bacteriol. 179:62016204.
4. Hantke, K.,, G. Nicholson,, W. Rabsch,, and G. Winkelmann. 2003. Salmochelins,new siderophores of Salmonella enterica and uropathogenic Escherichia coli strains,are recognized by the outer membrane receptor IroN. Proc. Natl. Acad. Sci. USA 100: 36773682.
5. Kammler, M.,, C. Schön,, and K. Hantke. 1993. Characterization of the ferrous iron uptake system of Escherichia coli. J. Bacteriol. 175:62126219.
6. Katoh, H.,, N. Hagino,, A. R. Grossman,, and T. Ogawa. 2001. Genes essential to iron transport in the cyanobacterium Synechocystis sp. strain PCC 6803. J. Bacteriol. 183:27792784.
7. Kim, C.,, W. W. Lorenz,, J. T. Hoopes,, and J. F. Dean. 2001. Oxidation of phenolate siderophores by the multicopper oxidase encoded by the Escherichia coli yacK gene. J. Bacteriol. 183:48664875.
8. Marlovits, T. C.,, W. Haase,, C. Herrmann,, S. G. Aller,, and V. M. Unger. 2002. The membrane protein FeoB contains an intramolecular G protein essential for Fe(II) uptake in bacteria. Proc. Natl. Acad. Sci. USA 99:1624316248.
9. May, J. J.,, T. M. Wendrich,, and M. A. Marahiel. 2001. The dhb operon of Bacillus subtilis encodes the biosynthetic template for the catecholic siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin. J. Biol. Chem. 276:72097217.
10. Outten, F. W.,, C. E. Outten,, J. Hale,, and T. V. O’Halloran. 2000. Transcriptional activation of an Escherichia coli copper efflux regulon by the chromosomal MerR homologue, cueR. J. Biol. Chem. 275: 3102431029.
11. Parkhill, J.,, B. W. Wren,, N. R. Thomson,, R. W. Titball,, M. T. Holden,, M. B. Prentice,, M. Sebaihia,, K. D. James,, C. Churcher,, K. L. Mungall,, S. Baker,, D. Basham,, S. D. Bentley,, K. Brooks,, A. M. Cerdeno-Tarraga,, T. Chillingworth,, A. Cronin,, R. M. Davies,, P. Davis,, G. Dougan,, T. Feltwell,, N. Hamlin,, S. Holroyd,, K. Jagels,, A. V. Karlyshev,, S. Leather,, S. Moule,, P. C. Oyston,, M. Quail,, K. Rutherford,, M. Simmonds,, J. Skelton,, K. Stevens,, S. Whitehead,, and B. G. Barrell. 2001. Genome sequence of Yersinia pestis,the causative agent of plague. Nature 413:523527.
12. Patzer, S. I.,, and K. Hantke. 1998. The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli. Mol. Microbiol. 28:11991210.
13. Pohl, E.,, R. K. Holmes,, and W. G. Hol. 1999. Crystal structure of a cobalt-activated diphtheria toxin repressor-DNA complex reveals a metal-binding SH3-like domain. J. Mol. Biol. 292:653667.
14. Roberts, S. A.,, A. Weichsel,, G. Grass,, K. Thakali,, J. T. Hazzard,, G. Tollin,, C. Rensing,, and W. R. Montfort. 2002. Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli. Proc. Natl. Acad. Sci. USA 99:27662771.
15. Robey, M.,, and N. P. Cianciotto. 2002. Legionella pneumophila feoAB promotes ferrous iron uptake and intracellular infection. Infect. Immun. 70:56595669.
16. Stojiljkovic, I.,, M. Cobeljic,, and K. Hantke. 1993. Escherichia coli K-12 ferrous iron uptake mutants are impaired in their ability to colonize the mouse intestine. FEMS Microbiol. Lett. 108:111115.
17. Tatusov, R. L.,, D. A. Natale,, I. V. Garkavtsev,, T. A. Tatusova,, U. T. Shankavaram,, B. S. Rao,, B. Kiryutin,, M. Y. Galperin,, N. D. Fedorova,, and E. V. Koonin. 2001. The COG database: new developments in phylogenetic classification of proteins from complete genomes. Nucleic Acids Res. 29:2228.
18. Tsolis, R. M.,, A. J. Baumler,, F. Heffron,, and I. Stojiljkovic. 1996. Contribution of TonB- and Feo-mediated iron uptake to growth of Salmonella typhimurium in the mouse. Infect. Immun. 64: 45494556.
19. Velayudhan, J.,, N. J. Hughes,, A. A. McColm,, J. Bagshaw,, C. L. Clayton,, S. C. Andrews,, and D. J. Kelly. 2000. Iron acquisition and virulence in Helicobacter pylori: a major role for FeoB,a high-affinity ferrous iron transporter. Mol. Microbiol. 37: 274286.
20. Waters, B. M.,, and D. J. Eide. 2002. Combinatorial control of yeast FET4 gene expression by iron, zinc, and oxygen. J. Biol. Chem. 277:3374933757.s

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