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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphatases / chemistry
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Adenosine Triphosphatases / genetics
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Adenosine Triphosphatases / isolation & purification
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Adenosine Triphosphatases / metabolism*
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Amino Acid Sequence
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Cell Cycle Proteins / chemistry
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Cell Cycle Proteins / genetics
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Cell Cycle Proteins / isolation & purification
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Cell Cycle Proteins / metabolism*
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Cell Division
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Cell Membrane / metabolism*
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Escherichia coli / cytology
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Escherichia coli / genetics*
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Escherichia coli / metabolism
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Escherichia coli Proteins / chemistry
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / isolation & purification
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Escherichia coli Proteins / metabolism*
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Kinetics
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Liposomes / chemistry
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Liposomes / metabolism
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Molecular Sequence Data
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Mutagenesis
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Mutation
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Protein Binding
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Sequence Alignment
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Sequence Homology, Amino Acid
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Solutions
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Static Electricity
Substances
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Cell Cycle Proteins
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Escherichia coli Proteins
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Liposomes
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MinE protein, E coli
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Solutions
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Adenosine Triphosphatases
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MinD protein, E coli