Metal Reduction and Protein Secretion Genes Required for Iodate Reduction by Shewanella oneidensis
Abstract
The metal-reducing gammaproteobacteriumShewanella oneidensisreduces iodate (IO3-) as an anaerobic terminal electron acceptor. Microbial IO3-electron transport pathways are postulated to terminate with nitrate (NO3-) reductase, which reduces IO3-as an alternative electron acceptor. Recent studies withS. oneidensis, however, have demonstrated that NO3-reductase is not involved in IO3-reduction. The main objective of the present study was to determine the metal reduction and protein secretion genes required for IO3-reduction byShewanella oneidensiswith lactate, formate, or H2as the electron donor. With all electron donors, the type I and type V protein secretion mutants retained wild-type IO3-reduction activity, while the type II protein secretion mutant lacking the outer membrane secretin GspD was impaired in IO3-reduction. Deletion mutants lacking the cyclic AMP receptor protein (CRP), cytochrome maturation permease CcmB, and inner membrane-tetheredc-type cytochrome CymA were impaired in IO3-reduction with all electron donors, while deletion mutants lackingc-type cytochrome MtrA and outer membrane β-barrel protein MtrB of the outer membrane MtrAB module were impaired in IO3-reduction with only lactate as an electron donor. With all electron donors, mutants lacking thec-type cytochromes OmcA and MtrC of the metal-reducing extracellular electron conduit MtrCAB retained wild-type IO3-reduction activity. These findings indicate that IO3-reduction byS. oneidensisinvolves electron donor-dependent metal reduction and protein secretion pathwaymore »
- Authors:
-
- Georgia Inst. of Technology, Atlanta, GA (United States)
- Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
- Savannah River National Lab., Aiken, SC (United States)
- Goethe Univ., Frankfurt am Main (Germany)
- Publication Date:
- Research Org.:
- Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 1501527
- Report Number(s):
- PNNL-SA-137826
Journal ID: ISSN 0099-2240
- Grant/Contract Number:
- AC05-76RL01830
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Applied and Environmental Microbiology
- Additional Journal Information:
- Journal Volume: 85; Journal Issue: 3; Journal ID: ISSN 0099-2240
- Publisher:
- American Society for Microbiology
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; 54 ENVIRONMENTAL SCIENCES; Shewanella oneidensis; iodate; iodine; metals; reduction
Citation Formats
Toporek, Yael J., Mok, Jung Kee, Shin, Hyun Dong, Lee, Brady D., Lee, M. Hope, DiChristina, Thomas J., and Müller, Volker. Metal Reduction and Protein Secretion Genes Required for Iodate Reduction by Shewanella oneidensis. United States: N. p., 2019.
Web. doi:10.1128/AEM.02115-18.
Toporek, Yael J., Mok, Jung Kee, Shin, Hyun Dong, Lee, Brady D., Lee, M. Hope, DiChristina, Thomas J., & Müller, Volker. Metal Reduction and Protein Secretion Genes Required for Iodate Reduction by Shewanella oneidensis. United States. https://doi.org/10.1128/AEM.02115-18
Toporek, Yael J., Mok, Jung Kee, Shin, Hyun Dong, Lee, Brady D., Lee, M. Hope, DiChristina, Thomas J., and Müller, Volker. Wed .
"Metal Reduction and Protein Secretion Genes Required for Iodate Reduction by Shewanella oneidensis". United States. https://doi.org/10.1128/AEM.02115-18. https://www.osti.gov/servlets/purl/1501527.
@article{osti_1501527,
title = {Metal Reduction and Protein Secretion Genes Required for Iodate Reduction by Shewanella oneidensis},
author = {Toporek, Yael J. and Mok, Jung Kee and Shin, Hyun Dong and Lee, Brady D. and Lee, M. Hope and DiChristina, Thomas J. and Müller, Volker},
abstractNote = {The metal-reducing gammaproteobacteriumShewanella oneidensisreduces iodate (IO3-) as an anaerobic terminal electron acceptor. Microbial IO3-electron transport pathways are postulated to terminate with nitrate (NO3-) reductase, which reduces IO3-as an alternative electron acceptor. Recent studies withS. oneidensis, however, have demonstrated that NO3-reductase is not involved in IO3-reduction. The main objective of the present study was to determine the metal reduction and protein secretion genes required for IO3-reduction byShewanella oneidensiswith lactate, formate, or H2as the electron donor. With all electron donors, the type I and type V protein secretion mutants retained wild-type IO3-reduction activity, while the type II protein secretion mutant lacking the outer membrane secretin GspD was impaired in IO3-reduction. Deletion mutants lacking the cyclic AMP receptor protein (CRP), cytochrome maturation permease CcmB, and inner membrane-tetheredc-type cytochrome CymA were impaired in IO3-reduction with all electron donors, while deletion mutants lackingc-type cytochrome MtrA and outer membrane β-barrel protein MtrB of the outer membrane MtrAB module were impaired in IO3-reduction with only lactate as an electron donor. With all electron donors, mutants lacking thec-type cytochromes OmcA and MtrC of the metal-reducing extracellular electron conduit MtrCAB retained wild-type IO3-reduction activity. These findings indicate that IO3-reduction byS. oneidensisinvolves electron donor-dependent metal reduction and protein secretion pathway components, including the outer membrane MtrAB module and type II protein secretion of an unidentified IO3-reductase to theS. oneidensisouter membrane.},
doi = {10.1128/AEM.02115-18},
journal = {Applied and Environmental Microbiology},
number = 3,
volume = 85,
place = {United States},
year = {2019},
month = {1}
}
Web of Science
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