A Ferrous Iron Exporter Mediates Iron Resistance in Shewanella oneidensis MR-1

Shewanella oneidensis strain MR-1 is a dissimilatory metal-reducing bacterium frequently found in aquatic sediments. In the absence of oxygen, S. oneidensis can respire extracellular, insoluble oxidized metals, such as iron (hydr)oxides, making it intimately involved in environmental metal and nutri...

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Published inApplied and Environmental Microbiology Vol. 81; no. 22; pp. 7938 - 7944
Main Authors Bennett, Brittany D., Brutinel, Evan D., Gralnick, Jeffrey A.
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.11.2015
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Abstract Shewanella oneidensis strain MR-1 is a dissimilatory metal-reducing bacterium frequently found in aquatic sediments. In the absence of oxygen, S. oneidensis can respire extracellular, insoluble oxidized metals, such as iron (hydr)oxides, making it intimately involved in environmental metal and nutrient cycling. The reduction of ferric iron (Fe 3+ ) results in the production of ferrous iron (Fe 2+ ) ions, which remain soluble under certain conditions and are toxic to cells at higher concentrations. We have identified an inner membrane protein in S. oneidensis , encoded by the gene SO_4475 and here called FeoE, which is important for survival during anaerobic iron respiration. FeoE, a member of the cation diffusion facilitator (CDF) protein family, functions to export excess Fe 2+ from the MR-1 cytoplasm. Mutants lacking feoE exhibit an increased sensitivity to Fe 2+ . The export function of FeoE is specific for Fe 2+ , as an feoE mutant is equally sensitive to other metal ions known to be substrates of other CDF proteins (Cd 2+ , Co 2+ , Cu 2+ , Mn 2+ , Ni 2+ , or Zn 2+ ). The substrate specificity of FeoE differs from that of FieF, the Escherichia coli homolog of FeoE, which has been reported to be a Cd 2+ /Zn 2+ or Fe 2+ /Zn 2+ exporter. A complemented feoE mutant has an increased growth rate in the presence of excess Fe 2+ compared to that of the Δ feoE mutant complemented with fieF . It is possible that FeoE has evolved to become an efficient and specific Fe 2+ exporter in response to the high levels of iron often present in the types of environmental niches in which Shewanella species can be found.
AbstractList Shewanella oneidensis strain MR-1 is a dissimilatory metal-reducing bacterium frequently found in aquatic sediments. In the absence of oxygen, S. oneidensis can respire extracellular, insoluble oxidized metals, such as iron (hydr)oxides, making it intimately involved in environmental metal and nutrient cycling. The reduction of ferric iron (Fe3+) results in the production of ferrous iron (Fe2+) ions, which remain soluble under certain conditions and are toxic to cells at higher concentrations. We have identified an inner membrane protein in S. oneidensis, encoded by the gene SO_4475 and here called FeoE, which is important for survival during anaerobic iron respiration. FeoE, a member of the cation diffusion facilitator (CDF) protein family, functions to export excess Fe2+ from the MR-1 cytoplasm. Mutants lacking feoE exhibit an increased sensitivity to Fe2+. The export function of FeoE is specific for Fe2+, as an feoE mutant is equally sensitive to other metal ions known to be substrates of other CDF proteins (Cd2+, Co2+, Cu2+, Mn2+, Ni2+, or Zn2+). The substrate specificity of FeoE differs from that of FieF, the Escherichia coli homolog of FeoE, which has been reported to be a Cd2+/Zn2+ or Fe2+/Zn2+ exporter. A complemented feoE mutant has an increased growth rate in the presence of excess Fe2+ compared to that of the Delta feoE mutant complemented with fieF. It is possible that FeoE has evolved to become an efficient and specific Fe2+ exporter in response to the high levels of iron often present in the types of environmental niches in which Shewanella species can be found.
Shewanella oneidensis strain MR-1 is a dissimilatory metal-reducing bacterium frequently found in aquatic sediments. In the absence of oxygen, S. oneidensis can respire extracellular, insoluble oxidized metals, such as iron (hydr)oxides, making it intimately involved in environmental metal and nutrient cycling. The reduction of ferric iron (Fe...) results in the production of ferrous iron (Fe...) ions, which remain soluble under certain conditions and are toxic to cells at higher concentrations. We have identified an inner membrane protein in S. oneidensis, encoded by the gene SO_4475 and here called FeoE, which is important for survival during anaerobic iron respiration. FeoE, a member of the cation diffusion facilitator (CDF) protein family, functions to export excess Fe... from the MR-1 cytoplasm. Mutants lacking feoE exhibit an increased sensitivity to Fe... The export function of FeoE is specific for Fe..., as an feoE mutant is equally sensitive to other metal ions known to be substrates of other CDF proteins (Cd..., Co..., Cu..., Mn..., Ni..., or Zn...). The substrate specificity of FeoE differs from that of FieF, the Escherichia coli homolog of FeoE, which has been reported to be a Cd.../Zn... or Fe.../Zn... exporter. A complemented feoE mutant has an increased growth rate in the presence of excess Fe... compared to that of the ...feoE mutant complemented with fieF. It is possible that FeoE has evolved to become an efficient and specific Fe... exporter in response to the high levels of iron often present in the types of environmental niches in which Shewanella species can be found. (ProQuest: ... denotes formulae/symbols omitted.)
Shewanella oneidensis strain MR-1 is a dissimilatory metal-reducing bacterium frequently found in aquatic sediments. In the absence of oxygen, S. oneidensis can respire extracellular, insoluble oxidized metals, such as iron (hydr)oxides, making it intimately involved in environmental metal and nutrient cycling. The reduction of ferric iron (Fe(3+)) results in the production of ferrous iron (Fe(2+)) ions, which remain soluble under certain conditions and are toxic to cells at higher concentrations. We have identified an inner membrane protein in S. oneidensis, encoded by the gene SO_4475 and here called FeoE, which is important for survival during anaerobic iron respiration. FeoE, a member of the cation diffusion facilitator (CDF) protein family, functions to export excess Fe(2+) from the MR-1 cytoplasm. Mutants lacking feoE exhibit an increased sensitivity to Fe(2+). The export function of FeoE is specific for Fe(2+), as an feoE mutant is equally sensitive to other metal ions known to be substrates of other CDF proteins (Cd(2+), Co(2+), Cu(2+), Mn(2+), Ni(2+), or Zn(2+)). The substrate specificity of FeoE differs from that of FieF, the Escherichia coli homolog of FeoE, which has been reported to be a Cd(2+)/Zn(2+) or Fe(2+)/Zn(2+) exporter. A complemented feoE mutant has an increased growth rate in the presence of excess Fe(2+) compared to that of the ΔfeoE mutant complemented with fieF. It is possible that FeoE has evolved to become an efficient and specific Fe(2+) exporter in response to the high levels of iron often present in the types of environmental niches in which Shewanella species can be found.
Shewanella oneidensis strain MR-1 is a dissimilatory metal-reducing bacterium frequently found in aquatic sediments. In the absence of oxygen, S. oneidensis can respire extracellular, insoluble oxidized metals, such as iron (hydr)oxides, making it intimately involved in environmental metal and nutrient cycling. The reduction of ferric iron (Fe(3+)) results in the production of ferrous iron (Fe(2+)) ions, which remain soluble under certain conditions and are toxic to cells at higher concentrations. We have identified an inner membrane protein in S. oneidensis, encoded by the gene SO_4475 and here called FeoE, which is important for survival during anaerobic iron respiration. FeoE, a member of the cation diffusion facilitator (CDF) protein family, functions to export excess Fe(2+) from the MR-1 cytoplasm. Mutants lacking feoE exhibit an increased sensitivity to Fe(2+). The export function of FeoE is specific for Fe(2+), as an feoE mutant is equally sensitive to other metal ions known to be substrates of other CDF proteins (Cd(2+), Co(2+), Cu(2+), Mn(2+), Ni(2+), or Zn(2+)). The substrate specificity of FeoE differs from that of FieF, the Escherichia coli homolog of FeoE, which has been reported to be a Cd(2+)/Zn(2+) or Fe(2+)/Zn(2+) exporter. A complemented feoE mutant has an increased growth rate in the presence of excess Fe(2+) compared to that of the ΔfeoE mutant complemented with fieF. It is possible that FeoE has evolved to become an efficient and specific Fe(2+) exporter in response to the high levels of iron often present in the types of environmental niches in which Shewanella species can be found.Shewanella oneidensis strain MR-1 is a dissimilatory metal-reducing bacterium frequently found in aquatic sediments. In the absence of oxygen, S. oneidensis can respire extracellular, insoluble oxidized metals, such as iron (hydr)oxides, making it intimately involved in environmental metal and nutrient cycling. The reduction of ferric iron (Fe(3+)) results in the production of ferrous iron (Fe(2+)) ions, which remain soluble under certain conditions and are toxic to cells at higher concentrations. We have identified an inner membrane protein in S. oneidensis, encoded by the gene SO_4475 and here called FeoE, which is important for survival during anaerobic iron respiration. FeoE, a member of the cation diffusion facilitator (CDF) protein family, functions to export excess Fe(2+) from the MR-1 cytoplasm. Mutants lacking feoE exhibit an increased sensitivity to Fe(2+). The export function of FeoE is specific for Fe(2+), as an feoE mutant is equally sensitive to other metal ions known to be substrates of other CDF proteins (Cd(2+), Co(2+), Cu(2+), Mn(2+), Ni(2+), or Zn(2+)). The substrate specificity of FeoE differs from that of FieF, the Escherichia coli homolog of FeoE, which has been reported to be a Cd(2+)/Zn(2+) or Fe(2+)/Zn(2+) exporter. A complemented feoE mutant has an increased growth rate in the presence of excess Fe(2+) compared to that of the ΔfeoE mutant complemented with fieF. It is possible that FeoE has evolved to become an efficient and specific Fe(2+) exporter in response to the high levels of iron often present in the types of environmental niches in which Shewanella species can be found.
Shewanella oneidensis strain MR-1 is a dissimilatory metal-reducing bacterium frequently found in aquatic sediments. In the absence of oxygen, S. oneidensis can respire extracellular, insoluble oxidized metals, such as iron (hydr)oxides, making it intimately involved in environmental metal and nutrient cycling. The reduction of ferric iron (Fe 3+ ) results in the production of ferrous iron (Fe 2+ ) ions, which remain soluble under certain conditions and are toxic to cells at higher concentrations. We have identified an inner membrane protein in S. oneidensis , encoded by the gene SO_4475 and here called FeoE, which is important for survival during anaerobic iron respiration. FeoE, a member of the cation diffusion facilitator (CDF) protein family, functions to export excess Fe 2+ from the MR-1 cytoplasm. Mutants lacking feoE exhibit an increased sensitivity to Fe 2+ . The export function of FeoE is specific for Fe 2+ , as an feoE mutant is equally sensitive to other metal ions known to be substrates of other CDF proteins (Cd 2+ , Co 2+ , Cu 2+ , Mn 2+ , Ni 2+ , or Zn 2+ ). The substrate specificity of FeoE differs from that of FieF, the Escherichia coli homolog of FeoE, which has been reported to be a Cd 2+ /Zn 2+ or Fe 2+ /Zn 2+ exporter. A complemented feoE mutant has an increased growth rate in the presence of excess Fe 2+ compared to that of the Δ feoE mutant complemented with fieF . It is possible that FeoE has evolved to become an efficient and specific Fe 2+ exporter in response to the high levels of iron often present in the types of environmental niches in which Shewanella species can be found.
Author Gralnick, Jeffrey A.
Bennett, Brittany D.
Brutinel, Evan D.
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Citation Bennett BD, Brutinel ED, Gralnick JA. 2015. A ferrous iron exporter mediates iron resistance in Shewanella oneidensis MR-1. Appl Environ Microbiol 81:7938–7944. doi:10.1128/AEM.02835-15.
Present address: Evan D. Brutinel, 3M Corporate Research Materials Laboratory, St. Paul, Minnesota, USA.
OpenAccessLink https://aem.asm.org/content/aem/81/22/7938.full.pdf
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Snippet Shewanella oneidensis strain MR-1 is a dissimilatory metal-reducing bacterium frequently found in aquatic sediments. In the absence of oxygen, S. oneidensis...
Shewanella oneidensis strain MR-1 is a dissimilatory metal-reducing bacterium frequently found in aquatic sediments. In the absence of oxygen, S. oneidensis...
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StartPage 7938
SubjectTerms Bacteria
Bacterial Outer Membrane Proteins - genetics
Bacterial Outer Membrane Proteins - metabolism
Cadmium
Diffusion
E coli
Escherichia coli
Ferrous Compounds - metabolism
Geomicrobiology
Ions
Iron
Iron - metabolism
Membranes
Metals
Mutants
Nutrient cycles
Oxidation-Reduction
Respiration
Sediments
Shewanella - genetics
Shewanella - metabolism
Shewanella oneidensis
Zinc
Title A Ferrous Iron Exporter Mediates Iron Resistance in Shewanella oneidensis MR-1
URI https://www.ncbi.nlm.nih.gov/pubmed/26341213
https://www.proquest.com/docview/1727411977
https://www.proquest.com/docview/1725522662
https://www.proquest.com/docview/1746892643
https://pubmed.ncbi.nlm.nih.gov/PMC4616933
Volume 81
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