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Mol Microbiol. 2015 Nov;98(4):727-42. doi: 10.1111/mmi.13152. Epub 2015 Sep 10.

The role of FlhF and HubP as polar landmark proteins in Shewanella putrefaciens CN-32.

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Department of Microbiology and Molecular Biology, Justus-Liebig Universität, 35392, Giessen, Germany.
Department of Ecophysiology, Max-Planck-Institut für terrestrische Mikrobiologie, 35043, Marburg, Germany.
LOEWE Center for Synthetic Microbiology (Synmikro) & Department of Chemistry, Philipps University Marburg, 35043, Marburg, Germany.


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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