Abstract
Many cell division-related proteins are located at specific positions in the bacterial cell, and this organized distribution of proteins requires energy. Here, we report that the proton motive force, or more specifically the (trans)membrane potential, is directly involved in protein localization. It emerged that the membrane potential modulates the distribution of several conserved cell division proteins such as MinD, FtsA, and the bacterial cytoskeletal protein MreB. We show for MinD that this is based on the membrane potential stimulated binding of its C-terminal amphipathic helix. This function of the membrane potential has implications for how these morphogenetic proteins work and provide an explanation for the effects observed with certain antimicrobial compounds.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphatases / genetics
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Adenosine Triphosphatases / metabolism
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Bacillus subtilis / cytology
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Bacillus subtilis / metabolism*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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Carbonyl Cyanide m-Chlorophenyl Hydrazone / pharmacology
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Cell Division*
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Escherichia coli / cytology
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Escherichia coli / metabolism*
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / metabolism
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Green Fluorescent Proteins / genetics
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Green Fluorescent Proteins / metabolism
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Ionophores / pharmacology
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Membrane Potentials
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Microscopy, Fluorescence
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Protein Transport / drug effects
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
Substances
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Bacterial Proteins
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Escherichia coli Proteins
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FtsA protein, Bacteria
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Ionophores
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Recombinant Fusion Proteins
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Green Fluorescent Proteins
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Carbonyl Cyanide m-Chlorophenyl Hydrazone
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Adenosine Triphosphatases
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MinD protein, E coli