Dynamic Assembly of MinD into Filament Bundles Modulated by ATP, Phospholipids, and MinE

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 unde...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2002-12, Vol.99 (26), p.16776-16781
Main Authors: Suefuji, Kyoko, Valluzzi, Regina, RayChaudhuri, Debabrata
Format: Article
Language:English
Subjects:
Adenosine triphosphatases
Adenosine Triphosphatases - chemistry
Adenosine Triphosphate - physiology
Bacteria
Biological Sciences
Cell Cycle Proteins
Cell division
Cell membranes
Cellular biology
Escherichia coli
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - physiology
Horseshoes
Hydrolysis
Lipids
Mental concentration
Microscopy, Electron
Phospholipids
Phospholipids - physiology
Polymerization
Polymers
Polymers - chemistry
Teeth
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Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.262671699