Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 99, Issue 26, Pages 16776-16781Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.262671699
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- NIDDK NIH HHS [P30 DK034928, P30 DK-34928] Funding Source: Medline
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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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