The MinDE system is a generic spatial cue for membrane protein distribution in vitro

Beatrice Ramm, Philipp Glock, Jonas Mücksch, Philipp Blumhardt, Daniela A. García-Soriano, Michael Heymann and Petra Schwille ()
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Beatrice Ramm: Max Planck Institute of Biochemistry
Philipp Glock: Max Planck Institute of Biochemistry
Jonas Mücksch: Max Planck Institute of Biochemistry
Philipp Blumhardt: Max Planck Institute of Biochemistry
Daniela A. García-Soriano: Max Planck Institute of Biochemistry
Michael Heymann: Max Planck Institute of Biochemistry
Petra Schwille: Max Planck Institute of Biochemistry

Nature Communications, 2018, vol. 9, issue 1, 1-16

Abstract: Abstract The E. coli MinCDE system has become a paradigmatic reaction–diffusion system in biology. The membrane-bound ATPase MinD and ATPase-activating protein MinE oscillate between the cell poles followed by MinC, thus positioning the main division protein FtsZ at midcell. Here we report that these energy-consuming MinDE oscillations may play a role beyond constraining MinC/FtsZ localization. Using an in vitro reconstitution assay, we show that MinDE self-organization can spatially regulate a variety of functionally completely unrelated membrane proteins into patterns and gradients. By concentration waves sweeping over the membrane, they induce a direct net transport of tightly membrane-attached molecules. That the MinDE system can spatiotemporally control a much larger set of proteins than previously known, may constitute a MinC-independent pathway to division site selection and chromosome segregation. Moreover, the here described phenomenon of active transport through a traveling diffusion barrier may point to a general mechanism of spatiotemporal regulation in cells.

Date: 2018
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DOI: 10.1038/s41467-018-06310-1

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