Proceedings of the National Academy of Sciences · 2010 · 552 citations · 31 references
Life SciencesBiophysicsMicrobiologyCytoskeletonMembrane BiophysicsProtein BiochemistryBacterial Cell StructureBiological MembranesMembrane PotentialMembrane ProteinsProtein StructureProton Motive ForceBacterial Cell DivisionBacterial Cytoskeletal OrganizationBacterial Proton Motive ForceProton Motive Force RegulationSubcellular Protein Localization
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.
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