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学術論文

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

MPS-Authors
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Ramm,  Beatrice
Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society;

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Glock,  Philipp
Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society;

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Mücksch,  Jonas
Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society;

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Blumhardt,  Philipp
Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society;

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Garcia-Soriano,  Daniela
Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society;

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Heymann,  Michael
Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society;

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Schwille,  Petra
Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society;

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Ramm_s41467-018-06310-1.pdf
(出版社版), 5MB

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引用

Ramm, B., Glock, P., Mücksch, J., Blumhardt, P., Garcia-Soriano, D., Heymann, M., & Schwille, P. (2018). The MinDE system is a generic spatial cue for membrane protein distribution in vitro. Nature Communications, 9:. doi:10.1038/s41467-018-06310-1.


引用: https://hdl.handle.net/21.11116/0000-0002-F333-2
要旨
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.