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  Stationary Patterns in a Two-Protein Reaction-Diffusion System

Glock, P., Ramm, B., Heermann, T., Kretschmer, S., Schweizer, J., Mücksch, J., et al. (2019). Stationary Patterns in a Two-Protein Reaction-Diffusion System. ACS Synthetic Biology, 8(1), 148-157. doi:10.1021/acssynbio.8b00415.

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 Creators:
Glock, Philipp1, Author              
Ramm, Beatrice1, Author              
Heermann, Tamara1, Author              
Kretschmer, Simon1, Author              
Schweizer, Jakob1, Author              
Mücksch, Jonas1, Author              
Alagöz, Gökberk1, Author              
Schwille, Petra1, Author              
Affiliations:
1Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565169              

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Free keywords: DIVISION REGULATOR MINE; BACILLUS-SUBTILIS; MEMBRANE-BINDING; SITE; OSCILLATION; SELECTION; PROTEINSBiochemistry & Molecular Biology; pattern formation; self-organization; in vitro reconstitution; min proteins; reaction-diffusion system; stationary pattern;
 Abstract: Patterns formed by reaction-diffusion mechanisms are crucial for the development or sustenance of most organisms in nature. Patterns include dynamic waves, but are more often found as static distributions, such as animal skin patterns. Yet, a simplistic biological model system to reproduce and quantitatively investigate static reaction-diffusion patterns has been missing so far. Here, we demonstrate that the Escherichia coli MM system, known for its oscillatory behavior between the cell poles, is under certain conditions capable of transitioning to quasi-stationary protein distributions on membranes closely resembling Turing patterns. We systematically titrated both proteins, MinD and MinE, and found that removing all purification tags and linkers from the N-terminus of MinE was critical for static patterns to occur. At small bulk heights, dynamic patterns dominate, such as in rod-shaped microcompartments. We see implications of this work for studying pattern formation in general, but also for creating artificial gradients as downstream cues in synthetic biology applications.

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Language(s): eng - English
 Dates: 2019
 Publication Status: Published in print
 Pages: 19
 Publishing info: -
 Table of Contents: We would like to thank Core Facility MPIB for help with protein purifications ...
 Rev. Type: -
 Identifiers: ISI: 000456633300015
DOI: 10.1021/acssynbio.8b00415
 Degree: -

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Title: ACS Synthetic Biology
  Abbreviation : ACS Synth. Biol.
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Chemical Society
Pages: - Volume / Issue: 8 (1) Sequence Number: - Start / End Page: 148 - 157 Identifier: ISSN: 2161-5063
CoNE: https://pure.mpg.de/cone/journals/resource/2161-5063