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.
Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
A division inhibitor and a topological specificity factor coded for by the minicell locus determine proper placement of the division septum in E. coli
Proper placement of the Escherichia coli division site requires two functions that are associated with different domains of the MinE protein
The dimerization and topological specificity functions of MinE reside in a structurally autonomous C-terminal domain
Topological regulation of cell division in E. coli. spatiotemporal oscillation of MinD requires stimulation of its ATPase by MinE and phospholipid
Division site placement in E.coli: mutations that prevent formation of the MinE ring lead to loss of the normal midcell arrest of growth of polar MinD membrane domains
Membrane localization of MinD is mediated by a C-terminal motif that is conserved across eubacteria, archaea, and chloroplasts
Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles
Membrane binding by MinD involves insertion of hydrophobic residues within the C-terminal amphipathic helix into the bilayer
Mapping the MinE site involved in interaction with the MinD division site selection protein of Escherichia coli
Positioning of the MinE binding site on the MinD surface suggests a plausible mechanism for activation of the Escherichia coli MinD ATPase during division site selection
Analysis of MinD mutations reveals residues required for MinE stimulation of the MinD ATPase and residues required for MinC interaction
The MreB and Min cytoskeletal-like systems play independent roles in prokaryotic polar differentiation
A Single-step Method for the Simultaneous Preparation of DNA, RNA, and Protein from Cells and Tissues
MinD and MinE interact with anionic phospholipids and regulate division plane formation in Escherichia coli.
The N-terminal amphipathic helix of the topological specificity factor MinE is associated with shaping membrane curvature
Toward Spatially Regulated Division of Protocells: Insights into the E. coli Min System from in Vitro Studies
Membrane-bound MinDE complex acts as a toggle switch that drives Min oscillation coupled to cytoplasmic depletion of MinD
Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC
Differential affinities of MinD and MinE to anionic phospholipid influence Min patterning dynamics in vitro
Highly canalized MinD transfer and MinE sequestration explain the origin of robust MinCDE-protein dynamics
The Min oscillator uses MinD-dependent conformational changes in MinE to spatially regulate cytokinesis
Molecular Interactions of the Min Protein System Reproduce Spatiotemporal Patterning in Growing and Dividing Escherichia coli Cells
Proteomic response of β-lactamases-producing Enterobacter cloacae complex strain to cefotaxime-induced stress
An Optimal Free Energy Dissipation Strategy of the MinCDE Oscillator in Regulating Symmetric Bacterial Cell Division
Quantitative Proteomics Analysis Reveals the Min System of Escherichia coli Modulates Reversible Protein Association with the Inner Membrane.
Dissecting the role of conformational change and membrane binding by the bacterial cell division regulator MinE in the stimulation of MinD ATPase activity
A cardiolipin-deficient mutant of Rhodobacter sphaeroides has an altered cell shape and is impaired in biofilm formation
MinC N- and C-Domain Interactions Modulate FtsZ Assembly, Division Site Selection, and MinD-Dependent Oscillation in Escherichia coli
Self-assembly of MinE on the membrane underlies formation of the MinE ring to sustain function of the Escherichia coli Min system.
Probing transient excited states of the bacterial cell division regulator MinE by relaxation dispersion NMR spectroscopy
Conformational equilibrium of MinE regulates the allowable concentration ranges of a protein wave for cell division
Atomic Force Microscopy Characterization of Protein Fibrils Formed by the Amyloidogenic Region of the Bacterial Protein MinE on Mica and a Supported Lipid Bilayer
The sequences of MinE responsible for its subcellular localization analyzed by competitive binding method in Escherichia coli
Cell-sized confinement controls generation and stability of a protein wave for spatiotemporal regulation in cells
Amyloidogenic Peptides in Human Neuro-Degenerative Diseases and in Microorganisms: A Sorrow Shared Is a Sorrow Halved?
Large-scale modulation of reconstituted Min protein patterns and gradients by defined mutations in MinE's membrane targeting sequence
De novo synthesized Min proteins drive oscillatory liposome deformation and regulate FtsA-FtsZ cytoskeletal patterns
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