High-Speed Atomic Force Microscopy Reveals the Inner Workings of the MinDE Protein Oscillator

Nano Letters
Atsushi MiyagiSimon Scheuring

Abstract

The MinDE protein system from E. coli has recently been identified as a minimal biological oscillator, based on two proteins only: The ATPase MinD and the ATPase activating protein MinE. In E. coli, the system works as the molecular ruler to place the divisome at midcell for cell division. Despite its compositional simplicity, the molecular mechanism leading to protein patterns and oscillations is still insufficiently understood. Here we used high-speed atomic force microscopy to analyze the mechanism of MinDE membrane association/dissociation dynamics on isolated membrane patches, down to the level of individual point oscillators. This nanoscale analysis shows that MinD association to and dissociation from the membrane are both highly cooperative but mechanistically different processes. We propose that they represent the two directions of a single allosteric switch leading to MinD filament formation and depolymerization. Association/dissociation are separated by rather long apparently silent periods. The membrane-associated period is characterized by MinD filament multivalent binding, avidity, while the dissociated period is defined by seeding of individual MinD. Analyzing association/dissociation kinetics with varying MinD an...Continue Reading

Citations

Nov 28, 2018·Nature Communications·George R Heath, Simon Scheuring
Sep 28, 2018·Nature Communications·Beatrice RammPetra Schwille
Jul 19, 2019·Cellular and Molecular Life Sciences : CMLS·Beatrice RammPetra Schwille
Feb 1, 2019·Journal of Cell Science·Kim J A VendelLiedewij Laan
Oct 10, 2020·Nature Communications·Fang JiaoSimon Scheuring

Related Concepts

MinD protein, E coli
MinE protein, E coli
DNA-dependent ATPase
Allosteric Regulation
Alkalescens-Dispar Group
Microscopy, Atomic Force
Cell Cycle Proteins
Escherichia coli Proteins
Polymerization
Allosteric Regulation

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