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      A Periplasmic Complex of the Nitrite Reductase NirS, the Chaperone DnaK, and the Flagellum Protein FliC Is Essential for Flagellum Assembly and Motility in Pseudomonas aeruginosa.

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          Abstract

          Pseudomonas aeruginosa is a ubiquitously occurring environmental bacterium and opportunistic pathogen responsible for various acute and chronic infections. Obviously, anaerobic energy generation via denitrification contributes to its ecological success. To investigate the structural basis for the interconnection of the denitrification machinery to other essential cellular processes, we have sought to identify the protein interaction partners of the denitrification enzyme nitrite reductase NirS in the periplasm. We employed NirS as an affinity-purifiable bait to identify interacting proteins in vivo. Results obtained revealed that both the flagellar structural protein FliC and the protein chaperone DnaK form a complex with NirS in the periplasm. The interacting domains of NirS and FliC were tentatively identified. The NirS-interacting stretch of amino acids lies within its cytochrome c domain. Motility assays and ultrastructure analyses revealed that a nirS mutant was defective in the formation of flagella and correspondingly in swimming motility. In contrast, the fliC mutant revealed an intact denitrification pathway. However, deletion of the nirF gene, coding for a heme d1 biosynthetic enzyme, which leads to catalytically inactive NirS, did not abolish swimming ability. This pointed to a structural function for the NirS protein. FliC and NirS were found colocalized with DnaK at the cell surface of P. aeruginosa. A function of the detected periplasmic NirS-DnaK-FliC complex in flagellum formation and motility was concluded and discussed.

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          Author and article information

          Journal
          J. Bacteriol.
          Journal of bacteriology
          American Society for Microbiology
          1098-5530
          0021-9193
          Oct 2015
          : 197
          : 19
          Affiliations
          [1 ] Institute of Microbiology, Technische Universität Braunschweig, Braunschweig, Niedersachsen, Germany Environmental Microbiology Laboratory, Helmholtz Center for Infection Research, Braunschweig, Niedersachsen, Germany.
          [2 ] Environmental Microbiology Laboratory, Helmholtz Center for Infection Research, Braunschweig, Niedersachsen, Germany Central Facility for Microscopy, Helmholtz Center for Infection Research, Braunschweig, Niedersachsen, Germany.
          [3 ] Central Facility for Microscopy, Helmholtz Center for Infection Research, Braunschweig, Niedersachsen, Germany.
          [4 ] Institute for Physical and Theoretical Chemistry-NanoBioSciences, Technische Universität Braunschweig, Braunschweig, Niedersachsen, Germany.
          [5 ] Cellular Proteome Research, Helmholtz Center for Infection Research, Braunschweig, Niedersachsen, Germany.
          [6 ] Environmental Microbiology Laboratory, Helmholtz Center for Infection Research, Braunschweig, Niedersachsen, Germany.
          [7 ] Institute of Microbiology, Technische Universität Braunschweig, Braunschweig, Niedersachsen, Germany.
          [8 ] Institute of Microbiology, Technische Universität Braunschweig, Braunschweig, Niedersachsen, Germany d.jahn@tu-bs.de.
          Article
          JB.00415-15
          10.1128/JB.00415-15
          4560289
          26170416
          99ade718-b447-4dcc-b76b-aa433f7122a8
          History

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