MinE conformational switching confers robustness on self-organized Min protein patterns

Proceedings of the National Academy of Sciences of the United States of America
Jonas DenkErwin Frey

Abstract

Protein patterning is vital for many fundamental cellular processes. This raises two intriguing questions: Can such intrinsically complex processes be reduced to certain core principles and, if so, what roles do the molecular details play in individual systems? A prototypical example for protein patterning is the bacterial Min system, in which self-organized pole-to-pole oscillations of MinCDE proteins guide the cell division machinery to midcell. These oscillations are based on cycling of the ATPase MinD and its activating protein MinE between the membrane and the cytoplasm. Recent biochemical evidence suggests that MinE undergoes a reversible, MinD-dependent conformational switch from a latent to a reactive state. However, the functional relevance of this switch for the Min network and pattern formation remains unclear. By combining mathematical modeling and in vitro reconstitution of mutant proteins, we dissect the two aspects of MinE's switch, persistent membrane binding and a change in MinE's affinity for MinD. Our study shows that the MinD-dependent change in MinE's binding affinity for MinD is essential for patterns to emerge over a broad and physiological range of protein concentrations. Mechanistically, our results sug...Continue Reading

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Aug 14, 2018·PLoS Computational Biology·Silke Bergeler, Erwin Frey
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Related Concepts

MinD protein, E coli
MinE protein, E coli
DNA-dependent ATPase
Striadyne
Cell Division Phases
Plasma Membrane
Protoplasm
Alkalescens-Dispar Group
Cell Surface Proteins
Theoretical Study

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