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 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.
Suefuji
Kyoko
K
Department of Molecular Biology and Microbiology, Tufts University School of Medicine, 136 Harrison Avenue, Boston, MA 02111, USA.
Valluzzi
Regina
R
RayChaudhuri
Debabrata
D
D000251:Adenosine Triphosphatases / Q000737:chemistry*; D000255:Adenosine Triphosphate / Q000502:physiology*; D018797:Cell Cycle Proteins; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000502:physiology*; D008854:Microscopy, Electron; D010743:Phospholipids / Q000502:physiology*; D011108:Polymers / Q000737:chemistry
D018797:Cell Cycle Proteins; D029968:Escherichia coli Proteins; C093548:MinE protein, E coli; D010743:Phospholipids; D011108:Polymers; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; C072069:MinD protein, E coli