Dynamic assembly of MinD into filament bundles modulated by ATP, phospholipids, and MinE

Proceedings of the National Academy of Sciences of the United States of America
Kyoko SuefujiD RayChaudhuri

Abstract

Accurate positioning of the division septum at the equator of Escherichia coli cells requires a rapid oscillation of MinD ATPase between the polar halves of the cell membrane, together with the division inhibitor MinC, under MinE control. The mechanism underlying MinD oscillation remains poorly understood. Here, we demonstrate that purified MinD assembles into protein filaments in the presence of ATP. Incubation with phospholipid vesicles further stimulates MinD polymerization. Addition of purified MinE in the presence of lipids promotes bundling of MinD filaments as well as their disassembly through activation of MinD ATPase. MinE thus provokes a net decay in the steady-state MinD polymer mass. Taken together, our results suggest that reversible MinD assembly modulated by MinE underlies the dynamic processing of positional information in E. coli to identify precisely the nascent site for cell division.

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Related Concepts

MinD protein, E coli
MinE protein, E coli
DNA-dependent ATPase
Striadyne
Electron Microscopy
Phospholipids
Polymers
Cell Cycle Proteins
Escherichia coli Proteins

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