Isolation of a High-Affinity Functional Protein Complex between OmcA and MtrC: Two Outer Membrane Decaheme
            <i>c</i>
            -Type Cytochromes of
            <i>Shewanella oneidensis</i>
            MR-1

Shi, Liang; Chen, Baowei; Wang, Zheming; Elias, Dwayne A.; Mayer, Michael; Gorby, Yuri A.; Ni, Shuison; Lower, Brian H.; Kennedy, David W.; Wunschel, David S.; Mottaz, Heather M.; Marshall, Matthew J.; Hill, Eric A.; Beliaev, Alex; Zachara, John M.; Fredrickson, James K.; Squier, Thomas C.

doi:10.1128/jb.01966-05

Cited by 230 publications

(247 citation statements)

References 46 publications

(66 reference statements)

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“…Our results demonstrate that MtrC and OmcA are required to produce electrically conductive nanowires and to transform hydrous ferric oxide into magnetite along extracellular structures that are morphologically identical to nanowires. Results correlating the loss of electrical conductivity, the (15). Investigations have suggested at least a partial overlap in the roles of these two cytochromes in the reduction of insoluble Mn(IV) oxide (16).…”

Section: Discussionmentioning

confidence: 99%

Electrically conductive bacterial nanowires produced by Shewanella oneidensis strain MR-1 and other microorganisms

Gorby

Yanina

McLean

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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Section: Discussionmentioning

confidence: 99%

Electrically conductive bacterial nanowires produced by Shewanella oneidensis strain MR-1 and other microorganisms

Gorby

Yanina

McLean

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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1,611

1,142

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“…47 Very recently Shi et al reported that OmcA and OmcB form a complex to facilitate electron transport in S. oneidensis. 48 In our experiments using SDS-PAGE separation of affinity purified, PIR labeled cell lysate, we repeatedly observed high MW (> 250 kD) bands as highlighted in the white box in Figure 3b. In-gel digestion and LC/MS/MS analysis identified both OmcA (MW 80 kD) and OmcB (MW 73 kD) proteins in this band.…”

Section: Discussionmentioning

confidence: 88%

Profiling the Membrane Proteome of Shewanella oneidensis MR-1 with New Affinity Labeling Probes

Tang

Munske

et al. 2006

J. Proteome Res.

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The membrane proteome plays a critical role in electron transport processes in Shewanella oneidensis MR-1, a bacterial organism that has great potential for bioremediation. Biotinylation of intact cells with subsequent affinity-enrichment has become a useful tool for characterization of the membrane proteome. As opposed to these commonly used, water-soluble commercial reagents, we here introduce a family of hydrophobic, cell-permeable affinity probes for extensive labeling and detection of membrane proteins. When applied to S. oneidensis cells, all three new chemical probes allowed identification of a substantial proportion of membrane proteins from total cell lysate without the use of specific membrane isolation method. From a total of 410 unique proteins identified, approximately 42% are cell envelope proteins that include outer membrane, periplasmic, and inner membrane proteins. This report demonstrates the first application of this intact cell biotinylation method to S. oneidensis and presents the results of many identified proteins that are involved in metal reduction processes. As a general labeling method, all chemical probes we introduced in this study can be extended to other organisms or cell types and will help expedite the characterization of membrane proteomes.

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“…For example, the translation elongation factor Tu has previously been observed as a contaminant in other proteomic studies. 13,42 After cell lysis, proteins are extracted into the buffer solution. In contrast to the native environment of intact cells, protein conformation and its interacting partners may change dramatically in the cell lysate solution.…”

Section: Discussionmentioning

confidence: 99%

“…13 Using "in vivo" cross-linking by formalde-hyde and Western blot, the OmcA-MtrC interaction has also been reported. 15 Despite recent advances made in understanding the roles of OmcA and MtrC in reduction of metals, the other components of the OmcA/MtrC-mediated electron transfer pathway have yet to be identified.…”

Section: Introductionmentioning

confidence: 99%

“…4-12 Purified OmcA and MtrC are functional metal reductases with the ability to bind and reduce solid metal oxide such as hematite. 8,13 In addition, OmcA and MtrC are directly involved in extracellular reduction of uranyl carbonate complexes to uraninite. 14 A previous study showed that MtrC was copurified with recombinant OmcA, and purified…”

Section: Introductionmentioning

confidence: 99%

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In Vivo Identification of the Outer Membrane Protein OmcA−MtrC Interaction Network in Shewanella oneidensis MR-1 Cells Using Novel Hydrophobic Chemical Cross-Linkers

et al. 2008

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Outer membrane (OM) cytochromes OmcA (SO1779) and MtrC (SO1778) are the integral components of electron transfer used by Shewanella oneidensis for anaerobic respiration of metal (hydr)oxides. Here the OmcA-MtrC interaction was identified in vivo using a novel hydrophobic chemical cross-linker (MRN) combined with immunoprecipitation techniques. In addition, identification of other OM proteins from the cross-linked complexes allows first visualization of the OmcA-MtrC interaction network. Further experiments on omcA and mtrC mutant cells showed OmcA plays a central role in the network interaction. For comparison, two commercial cross-linkers were also used in parallel, and both resulted in fewer OM protein identifications, indicating the superior properties of MRN for identification of membrane protein interactions. Finally, comparison experiments of in vivo cross-linking and cell lysate cross-linking resulted in significantly different protein interaction data, demonstrating the importance of in vivo cross-linking for study of proteinprotein interactions in cells.

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Isolation of a High-Affinity Functional Protein Complex between OmcA and MtrC: Two Outer Membrane Decaheme c -Type Cytochromes of Shewanella oneidensis MR-1

Cited by 230 publications

References 46 publications

Electrically conductive bacterial nanowires produced by Shewanella oneidensis strain MR-1 and other microorganisms

Electrically conductive bacterial nanowires produced by Shewanella oneidensis strain MR-1 and other microorganisms

Profiling the Membrane Proteome of Shewanella oneidensis MR-1 with New Affinity Labeling Probes

In Vivo Identification of the Outer Membrane Protein OmcA−MtrC Interaction Network in Shewanella oneidensis MR-1 Cells Using Novel Hydrophobic Chemical Cross-Linkers

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