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The role of FlhF and HubP as polar landmark proteins in Shewanella putrefaciens CN-32.
Rossmann, Florian; Brenzinger, Susanne; Knauer, Carina; Dörrich, Anja K; Bubendorfer, Sebastian; Ruppert, Ulrike; Bange, Gert; Thormann, Kai M.
Afiliación
  • Rossmann F; Department of Microbiology and Molecular Biology, Justus-Liebig Universität, 35392, Giessen, Germany.
  • Brenzinger S; Department of Ecophysiology, Max-Planck-Institut für terrestrische Mikrobiologie, 35043, Marburg, Germany.
  • Knauer C; Department of Microbiology and Molecular Biology, Justus-Liebig Universität, 35392, Giessen, Germany.
  • Dörrich AK; Department of Ecophysiology, Max-Planck-Institut für terrestrische Mikrobiologie, 35043, Marburg, Germany.
  • Bubendorfer S; LOEWE Center for Synthetic Microbiology (Synmikro) & Department of Chemistry, Philipps University Marburg, 35043, Marburg, Germany.
  • Ruppert U; Department of Microbiology and Molecular Biology, Justus-Liebig Universität, 35392, Giessen, Germany.
  • Bange G; Department of Microbiology and Molecular Biology, Justus-Liebig Universität, 35392, Giessen, Germany.
  • Thormann KM; Department of Microbiology and Molecular Biology, Justus-Liebig Universität, 35392, Giessen, Germany.
Mol Microbiol ; 98(4): 727-42, 2015 Nov.
Article en En | MEDLINE | ID: mdl-26235439
Spatiotemporal regulation of cell polarity plays a role in many fundamental processes in bacteria and often relies on 'landmark' proteins which recruit the corresponding clients to their designated position. Here, we explored the localization of two multi-protein complexes, the polar flagellar motor and the chemotaxis array, in Shewanella putrefaciens CN-32. We demonstrate that polar positioning of the flagellar system, but not of the chemotaxis system, depends on the GTPase FlhF. In contrast, the chemotaxis array is recruited by a transmembrane protein which we identified as the functional ortholog of Vibrio cholerae HubP. Mediated by its periplasmic N-terminal LysM domain, SpHubP exhibits an FlhF-independent localization pattern during cell cycle similar to its Vibrio counterpart and also has a role in proper chromosome segregation. In addition, while not affecting flagellar positioning, SpHubP is crucial for normal flagellar function and is involved in type IV pili-mediated twitching motility. We hypothesize that a group of HubP/FimV homologs, characterized by a rather conserved N-terminal periplasmic section required for polar targeting and a highly variable acidic cytoplasmic part, primarily mediating recruitment of client proteins, serves as polar markers in various bacterial species with respect to different cellular functions.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Shewanella putrefaciens / Proteínas de Unión al GTP Monoméricas / Flagelos Tipo de estudio: Prognostic_studies Idioma: En Revista: Mol Microbiol Asunto de la revista: BIOLOGIA MOLECULAR / MICROBIOLOGIA Año: 2015 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Shewanella putrefaciens / Proteínas de Unión al GTP Monoméricas / Flagelos Tipo de estudio: Prognostic_studies Idioma: En Revista: Mol Microbiol Asunto de la revista: BIOLOGIA MOLECULAR / MICROBIOLOGIA Año: 2015 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido