Large-scale modulation of reconstituted Min protein patterns and gradients by defined mutations in MinE's membrane targeting sequence

The E. coli MinDE oscillator is a paradigm for protein self-organization and gradient formation. Previously, we reconstituted Min protein wave patterns on flat membranes as well as gradient-forming pole-to-pole oscillations in cell-shaped PDMS microcompartments. These oscillations appeared to requir...

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Bibliographic Details
Published in:PloS one 2017-06, Vol.12 (6), p.e0179582-e0179582
Main Authors: Kretschmer, Simon, Zieske, Katja, Schwille, Petra
Format: Article
Language:English
Subjects:
Adenosine triphosphatase
Adenosine Triphosphatases - genetics
Adenosine Triphosphatases - metabolism
ATPases
Binding
Biochemistry
Biological Clocks - physiology
Biology
Biology and Life Sciences
Biophysics
Cell Cycle Proteins - genetics
Cell Cycle Proteins - metabolism
Cell division
Compartments
E coli
Escherichia coli - genetics
Escherichia coli - metabolism
Escherichia coli Proteins - genetics
Escherichia coli Proteins - metabolism
Forming
Gene mutation
Genetic aspects
Geometry
Lipids
Localization
Membrane Microdomains - genetics
Membrane Microdomains - metabolism
Membranes
Min protein
Modulation
Mutants
Mutation
Oscillations
Physical Sciences
Physiological aspects
Protein Binding - genetics
Protein structure
Proteins
Research and analysis methods
Robustness
Silicone resins
Studies
Versatility
Wavelength
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Summary:The E. coli MinDE oscillator is a paradigm for protein self-organization and gradient formation. Previously, we reconstituted Min protein wave patterns on flat membranes as well as gradient-forming pole-to-pole oscillations in cell-shaped PDMS microcompartments. These oscillations appeared to require direct membrane interaction of the ATPase activating protein MinE. However, it remained unclear how exactly Min protein dynamics are regulated by MinE membrane binding. Here, we dissect the role of MinE's membrane targeting sequence (MTS) by reconstituting various MinE mutants in 2D and 3D geometries. We demonstrate that the MTS defines the lower limit of the concentration-dependent wavelength of Min protein patterns while restraining MinE's ability to stimulate MinD's ATPase activity. Strikingly, a markedly reduced length scale-obtainable even by single mutations-is associated with a rich variety of multistable dynamic modes in cell-shaped compartments. This dramatic remodeling in response to biochemical changes reveals a remarkable trade-off between robustness and versatility of the Min oscillator.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0179582