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.
All microscopy raw data and simulation files (Mathematica and COMSOL) have been deposited in the Max Planck data service Edmond under the following URL:https://edmond.mpdl.mpg.de/imeji/collection/wGSlUmjVMnvxStN
Design of biochemical pattern forming systems from minimal motifs - microscopy and additional dataEdmond, wGSlUmjVMnvxStN.
- 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.
- Pierre Sens, Institut Curie, PSL Research University, CNRS, France
© 2019, Glock et al.
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.
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