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 in | Applied and Environmental Microbiology Vol. 81; no. 22; pp. 7938 - 7944 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
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. |
Author_xml | – sequence: 1 givenname: Brittany D. surname: Bennett fullname: Bennett, Brittany D. organization: BioTechnology Institute and Department of Microbiology, University of Minnesota—Twin Cities, St. Paul, Minnesota, USA – sequence: 2 givenname: Evan D. surname: Brutinel fullname: Brutinel, Evan D. organization: BioTechnology Institute and Department of Microbiology, University of Minnesota—Twin Cities, St. Paul, Minnesota, USA – sequence: 3 givenname: Jeffrey A. surname: Gralnick fullname: Gralnick, Jeffrey A. organization: BioTechnology Institute and Department of Microbiology, University of Minnesota—Twin Cities, St. Paul, Minnesota, USA |
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Copyright | Copyright © 2015, American Society for Microbiology. All Rights Reserved. Copyright American Society for Microbiology Nov 2015 Copyright © 2015, American Society for Microbiology. All Rights Reserved. 2015 American Society for Microbiology |
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DocumentTitleAlternate | FeoE in S. oneidensis MR-1 |
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Notes | SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 14 ObjectType-Article-1 ObjectType-Feature-2 content type line 23 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. |
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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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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 |
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