Regulation of dynamic polarity switching in bacteria by a Ras-like G-protein 
and its cognate GAP

Leonardy, S.; Miertzschke, M.; Bulyha, I.; Sperling, E.; Wittinghofer, A.; Sogaard-Andersen, L.

doi:10.1038/emboj.2010.114

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Regulation of dynamic polarity switching in bacteria by a Ras-like G-protein and its cognate GAP

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

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

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Sperling, E.
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

Leonardy, S., Miertzschke, M., Bulyha, I., Sperling, E., Wittinghofer, A., & Sogaard-Andersen, L. (2010). Regulation of dynamic polarity switching in bacteria by a Ras-like G-protein and its cognate GAP. EMBO Journal, 29(14), 2276-2289. doi:10.1038/emboj.2010.114.

Cite as: https://hdl.handle.net/21.11116/0000-0007-C343-1

Abstract

The rod-shaped cells of the bacterium Myxococcus xanthus move uni-directionally and occasionally undergo reversals during which the leading/lagging polarity axis is inverted. Cellular reversals depend on pole-to-pole relocation of motility proteins that localize to the cell poles between reversals. We show that MglA is a Ras-like G-protein and acts as a nucleotide-dependent molecular switch to regulate motility and that MglB represents a novel GTPase-activating protein (GAP) family and is the cognate GAP of MglA. Between reversals, MglA/GTP is restricted to the leading and MglB to the lagging pole defining the leading/lagging polarity axis. For reversals, the Frz chemosensory system induces the relocation of MglA/GTP to the lagging pole causing an inversion of the leading/lagging polarity axis. MglA/GTP stimulates motility by establishing correct polarity of motility proteins between reversals and reversals by inducing their pole-to-pole relocation. Thus, the function of Ras-like G-proteins and their GAPs in regulating cell polarity is found not only in eukaryotes, but also conserved in bacteria.