The N-terminal amphipathic helix of the topological specificity factor MinE is associated with shaping membrane curvature.

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 MinE(2-9), 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

SUBMITTER: Shih YL 

PROVIDER: S-EPMC3124506 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature