Abstract
Pole-to-pole oscillations of the Min proteins in Escherichia coli are required for the proper placement of the division septum. Direct interaction of MinE with the cell membrane is critical for the dynamic behavior of the Min system. In vitro, this MinE-membrane interaction led to membrane deformation; however, the underlying mechanism remained unclear. Here we report that MinE-induced membrane deformation involves the formation of an amphipathic helix of MinE2–9, which, together with the adjacent basic residues, function as membrane anchors. Biochemical evidence suggested that the membrane association induces formation of the helix, with the helical face, consisting of A2, L3, and F6, inserted into the membrane. Insertion of this helix into the cell membrane can influence local membrane curvature and lead to drastic changes in membrane topology. Accordingly, MinE showed characteristic features of protein-induced membrane tubulation and lipid clustering in in vitro reconstituted systems. In conclusion, MinE shares common protein signatures with a group of membrane trafficking proteins in eukaryotic cells. These MinE signatures appear to affect membrane curvature.
Highlights
Targeting of proteins to specific destinations at the appropriate time is crucial for cell function
In Escherichia coli (Ec), the position of the FtsZ ring is regulated by the Min system [2], which is composed of three proteins, MinC, MinD, and MinE; these cooperate to form a dynamic oscillator that guides the placement of the FtsZ assembly
The results suggest that the helical face of MinE, consisting of A2, L3, and F6, forms a hydrophobic surface that is oriented to interact with the hydrophobic regions of the phospholipid bilayer
Summary
Targeting of proteins to specific destinations at the appropriate time is crucial for cell function. This process often involves specific protein motifs, and requires the intricate regulation and coordination of different cellular components. Protein targeting is involved in prokaryotic cell division, during which a series of proteins are assembled in a hierarchical order to form a division septum at the correct mid-cell position. In Escherichia coli (Ec), the position of the FtsZ ring is regulated by the Min system [2], which is composed of three proteins, MinC, MinD, and MinE; these cooperate to form a dynamic oscillator that guides the placement of the FtsZ assembly. The underlying mechanisms responsible for the membrane-association properties of the Min system require further investigation
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