4.8 Article

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

Journal

NATURE COMMUNICATIONS
Volume 9, Issue -, Pages -

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-018-06310-1

Keywords

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Funding

  1. DFG fellowship through the Graduate School of Quantitative Biosciences Munich (QBM)
  2. DFG Collaborative Research Centre Spatiotemporal dynamics of bacterial cells [TRR 174/2017]
  3. MaxSynBio via German Federal Ministry of Education and Research (BMBF)
  4. Max Planck Society
  5. excellence cluster Nanosystems Initiative Munich
  6. International Max Planck Research School for Molecular Life Sciences
  7. Joachim Herz Foundation through an Add-on Fellowship
  8. Center for NanoScience Munich
  9. [GRK 2062]

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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.

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