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  Increasing MinD's Membrane Affinity Yields Standing Wave Oscillations and Functional Gradients on Flat Membranes

Kretschmer, S., Heermann, T., Tassinari, A., Glock, P., & Schwille, P. (2021). Increasing MinD's Membrane Affinity Yields Standing Wave Oscillations and Functional Gradients on Flat Membranes. ACS Synthetic Biology, 10(5), 939-949. doi:10.1021/acssynbio.0c00604.

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Genre: Journal Article

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 Creators:
Kretschmer, Simon1, Author              
Heermann, Tamara1, Author              
Tassinari, Andrea1, Author              
Glock, Philipp1, 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 INHIBITOR MINC; CELL-DIVISION; ESCHERICHIA-COLI; TOPOLOGICAL REGULATION; POLE OSCILLATION; BINDING; RECONSTITUTION; PROTEINS; SEQUENCEBiochemistry & Molecular Biology; pattern formation; pattern engineering; self-organization; in vitro reconstitution; reaction-diffusion system; Min proteins;
 Abstract: The formation of large-scale patterns through molecular self-organization is a basic principle of life. Accordingly, the engineering of protein patterns and gradients is of prime relevance for synthetic biology. As a paradigm for such pattern formation, the bacterial MinDE protein system is based on self-organization of the ATPase MinD and ATPase-activating protein MinE on lipid membranes. Min patterns can be tightly regulated by tuning physical or biochemical parameters. Among the biochemically engineerable modules, MinD's membrane targeting sequence, despite being a key regulating element, has received little attention. Here we attempt to engineer patterns by modulating the membrane affinity of MinD. Unlike the traveling waves or stationary patterns commonly observed in vitro on flat supported membranes, standing-wave oscillations emerge upon elongating MinD's membrane targeting sequence via rationally guided mutagenesis. These patterns are capable of forming gradients and thereby spatially target co-reconstituted downstream proteins, highlighting their functional potential in designing new life-like systems.

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Language(s): eng - English
 Dates: 2021
 Publication Status: Published in print
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000656057600004
DOI: 10.1021/acssynbio.0c00604
 Degree: -

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Title: ACS Synthetic Biology
  Abbreviation : ACS Synth. Biol.
Source Genre: Journal
 Creator(s):
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Publ. Info: Washington, D.C. : American Chemical Society
Pages: - Volume / Issue: 10 (5) Sequence Number: - Start / End Page: 939 - 949 Identifier: ISSN: 2161-5063
CoNE: https://pure.mpg.de/cone/journals/resource/2161-5063