Design of biochemical pattern forming systems from minimal motifs

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Cite this article as: eLife 2019;8:e48646 doi: 10.7554/eLife.48646

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Abstract

Although molecular self-organization and pattern formation are key features of life, only very few pattern-forming biochemical systems have been identified that can be reconstituted and studied in vitro under defined conditions. A systematic understanding of the underlying mechanisms is often hampered by multiple interactions, conformational flexibility and other complex features of the pattern forming proteins. Because of its compositional simplicity of only two proteins and a membrane, the MinDE system from Escherichia coli has in the past years been invaluable for deciphering the mechanisms of spatiotemporal self-organization in cells. Here we explored the potential of reducing the complexity of this system even further, by identifying key functional motifs in the effector MinE that could be used to design pattern formation from scratch. In a combined approach of experiment and quantitative modeling, we show that starting from a minimal MinE-MinD interaction motif, pattern formation can be obtained by adding either dimerization or membrane-binding motifs. Moreover, we show that the pathways underlying pattern formation are recruitment-driven cytosolic cycling of MinE and recombination of membrane-bound MinE, and that these differ in their in vivo phenomenology.

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Philipp Glock

Department of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Martinsried, Germany

Competing interests
The authors declare that no competing interests exist.

"This ORCID iD identifies the author of this article:" 0000-0002-0238-2634
Fridtjof Brauns

Arnold Sommerfeld Center for Theoretical Physics and Center for NanoScience, Department of Physics, Ludwig-Maximilians-Universität München, München, Germany

Competing interests
The authors declare that no competing interests exist.
Jacob Halatek

Arnold Sommerfeld Center for Theoretical Physics and Center for NanoScience, Department of Physics, Ludwig-Maximilians-Universität München, München, Germany

Competing interests
The authors declare that no competing interests exist.
Erwin Frey

Arnold Sommerfeld Center for Theoretical Physics and Center for NanoScience, Department of Physics, Ludwig-Maximilians-Universität München, München, Germany

For correspondence
frey@lmu.de

Competing interests
The authors declare that no competing interests exist.

"This ORCID iD identifies the author of this article:" 0000-0001-8792-3358
Petra Schwille

Department of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Martinsried, Germany

For correspondence
schwille@biochem.mpg.de

Competing interests
The authors declare that no competing interests exist.

"This ORCID iD identifies the author of this article:" 0000-0002-6106-4847

Funding

Deutsche Forschungsgemeinschaft (GRK2062)

Philipp Glock
Fridtjof Brauns
Erwin Frey
Petra Schwille

The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.

Reviewing Editor

Pierre Sens, Institut Curie, PSL Research University, CNRS, France

Publication history

Received: May 21, 2019
Accepted: November 6, 2019
Accepted Manuscript published: November 26, 2019 (version 1)

Copyright

This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.