Direct MinE-membrane interaction contributes to the proper localization of MinDE in E. coli

Molecular Microbiology
Cheng-Wei HsiehYu-Ling Shih

Abstract

Dynamic oscillation of the Min system in Escherichia coli determines the placement of the division plane at the midcell. In addition to stimulating MinD ATPase activity, we report here that MinE can directly interact with the membrane and this interaction contributes to the proper MinDE localization and dynamics. The N-terminal domain of MinE is involved in direct contact between MinE and the membranes that may subsequently be stabilized by the C-terminal domain of MinE. In an in vitro system, MinE caused liposome deformation into membrane tubules, a property similar to that previously reported for MinD. We isolated a mutant MinE containing residue substitutions in R10, K11 and K12 that was fully capable of stimulating MinD ATPase activity, but was deficient in membrane binding. Importantly, this mutant was unable to support normal MinDE localization and oscillation, suggesting that direct MinE interaction with the membrane is critical for the dynamic behavior of the Min system.

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Related Concepts

MinD protein, E coli
MinE protein, E coli
DNA-dependent ATPase
Cell Division Phases
Plasma Membrane
Alkalescens-Dispar Group
Niosomes
Plasma Protein Binding Capacity
Solutions
Mutagenesis Process

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