Metal Reduction and Protein Secretion Genes Required for Iodate Reduction by Shewanella oneidensis

• Published in: Applied and environmental microbiology 2019-02, Vol.85 (3)
• Main Authors: Toporek, Yael J, Mok, Jung Kee, Shin, Hyun Dong, Lee, Brady D, Lee, M Hope, DiChristina, Thomas J
• Format: Article
• Language: English
• Subjects: Anaerobic microorganisms; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; BASIC BIOLOGICAL SCIENCES; Biodegradation, Environmental; Cyclic AMP; Cyclic AMP receptor protein; Cyclic AMP Receptor Protein - genetics; Cyclic AMP Receptor Protein - metabolism; Cytochrome; Cytochrome c Group - metabolism; Cytochromes; Deletion mutant; Electron transport; ENVIRONMENTAL SCIENCES; Formates - metabolism; Genes; Geomicrobiology; iodate; Iodates - metabolism; iodine; Lactic acid; Lactic Acid - metabolism; Membrane proteins; Metals; Metals - metabolism; Microorganisms; Modules; Mutants; Nitrate Reductase - genetics; Nitrate Reductase - metabolism; Nitrates; Oxidation-Reduction; Permease; Proteins; Reductase; Reduction; Reduction (metal working); Secretin; Secretion; Shewanella - genetics; Shewanella - metabolism; Shewanella oneidensis; V protein
• ISSN: 0099-2240; 1098-5336
• DOI: 10.1128/AEM.02115-18

The metal-reducing gammaproteobacterium reduces iodate (IO ) as an anaerobic terminal electron acceptor. Microbial IO electron transport pathways are postulated to terminate with nitrate (NO ) reductase, which reduces IO as an alternative electron acceptor. Recent studies with , however, have demonstrated that NO reductase is not involved in IO reduction. The main objective of the present study was to determine the metal reduction and protein secretion genes required for IO reduction by with lactate, formate, or H as the electron donor. With all electron donors, the type I and type V protein secretion mutants retained wild-type IO reduction activity, while the type II protein secretion mutant lacking the outer membrane secretin GspD was impaired in IO reduction. Deletion mutants lacking the cyclic AMP receptor protein (CRP), cytochrome maturation permease CcmB, and inner membrane-tethered -type cytochrome CymA were impaired in IO reduction with all electron donors, while deletion mutants lacking -type cytochrome MtrA and outer membrane β-barrel protein MtrB of the outer membrane MtrAB module were impaired in IO reduction with only lactate as an electron donor. With all electron donors, mutants lacking the -type cytochromes OmcA and MtrC of the metal-reducing extracellular electron conduit MtrCAB retained wild-type IO reduction activity. These findings indicate that IO reduction by involves electron donor-dependent metal reduction and protein secretion pathway components, including the outer membrane MtrAB module and type II protein secretion of an unidentified IO reductase to the outer membrane. Microbial iodate (IO ) reduction is a major component in the biogeochemical cycling of iodine and the bioremediation of iodine-contaminated environments; however, the molecular mechanism of microbial IO reduction is poorly understood. Results of the present study indicate that outer membrane (type II) protein secretion and metal reduction genes encoding the outer membrane MtrAB module of the extracellular electron conduit MtrCAB are required for IO reduction by On the other hand, the metal-reducing -type cytochrome MtrC of the extracellular electron conduit is not required for IO reduction by These findings indicate that the IO electron transport pathway terminates with an as yet unidentified IO reductase that associates with the outer membrane MtrAB module to deliver electrons extracellularly to IO