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Regulation of Bacterial Cell Polarity by Small GTPases

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Keilberg,  D.
Bacterial Adaption and Differentiation, Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Sogaard-Andersen,  L.
Bacterial Adaption and Differentiation, Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Citation

Keilberg, D., & Sogaard-Andersen, L. (2014). Regulation of Bacterial Cell Polarity by Small GTPases. Biochemistry, 53(12), 1899-1907. doi:10.1021/bi500141f.


Cite as: https://hdl.handle.net/21.11116/0000-0007-BE25-A
Abstract
Bacteria are polarized with many proteins localizing dynamically to specific subcellular sites. Two GTPase families have important functions in the regulation of bacterial cell polarity, FlhF homologues and small GTPases of the Ras superfamily. The latter consist of only a G domain and are widespread in bacteria. The rod-shaped Myxococcus xanthus cells have two motility systems, one for gliding and one that depends on type IV pili. The function of both systems hinges on proteins that localize asymmetrically to the cell poles. During cellular reversals, these asymmetrically localized proteins are released from their respective poles and then bind to the opposite pole, resulting in an inversion of cell polarity. Here, we review genetic, cell biological, and biochemical analyses that identified two modules containing small Ras-like GTPases that regulate the dynamic polarity of motility proteins. The GTPase SofG interacts directly with the bactofilin cytoskeletal protein BacP to ensure polar localization of type IV pili proteins. In the second module, the small GTPase MglA, its cognate GTPase activating protein (GAP) MglB, and the response regulator RomR localize asymmetrically to the poles and sort dynamically localized motility proteins to the poles. During reversals, MglA, MglB, and RomR switch poles, in that way inducing the relocation of dynamically localized motility proteins. Structural analyses have demonstrated that MglB has a Roadblock/LC7 fold, the central β2 strand in MglA undergoes an unusual screw-type movement upon GTP binding, MglA contains an intrinsic Arg finger required for GTP hydrolysis, and MglA and MglB form an unusual G protein/GAP complex with a 1:2 stoichiometry.