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

Kyoko Suefuji¹, Regina Valluzzi, Debabrata RayChaudhuri

¹Department of Molecular Biology and Microbiology, Tufts University School of Medicine, 136 Harrison Avenue, Boston, MA 02111, USA.

Proceedings of the National Academy of Sciences of the United States of America

|December 17, 2002

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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Abstract:

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