Optical Control of a Biological Reaction-Diffusion System

Glock, Philipp; Broichhagen, Johannes; Kretschmer, Simon; Blumhardt, Philipp; Mücksch, Jonas; Trauner, Dirk; Schwille, P.

doi:10.1002/anie.201712002

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Optical Control of a Biological Reaction-Diffusion System

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

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Kretschmer, Simon
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;

/persons/resource/persons138355

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

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

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引用

Glock, P., Broichhagen, J., Kretschmer, S., Blumhardt, P., Mücksch, J., Trauner, D., & Schwille, P. (2018). Optical Control of a Biological Reaction-Diffusion System. Angewandte Chemie International Edition, 57(9), 2362-2366. doi:10.1002/anie.201712002.

引用: https://hdl.handle.net/21.11116/0000-0000-F6A1-4

要旨

Patterns formed by reaction and diffusion are the foundation for many phenomena in biology. However, the experimental study of reaction-diffusion (R-D) systems has so far been dominated by chemical oscillators, for which many tools are available. In this work, we developed a photoswitch for the Min system of Escherichia coli, a versatile biological in vitro R-D system consisting of the antagonistic proteins MinD and MinE. A MinE-derived peptide of 19 amino acids was covalently modified with a photoisomerizable crosslinker based on azobenzene to externally control peptide-mediated depletion of MinD from the membrane. In addition to providing an on-off switch for pattern formation, we achieve frequency-locked resonance with a precise 2D spatial memory, thus allowing new insights into Min protein action on the membrane. Taken together, we provide a tool to study phenomena in pattern formation using biological agents.