The N-Terminal Amphipathic Helix of the Topological Specificity Factor MinE Is Associated with Shaping Membrane Curvature
Resource
PLOS ONE, 6(6), e21425
Journal
PLoS ONE
Pages
e21425
Date Issued
2011
Date
2011
Author(s)
Shih, Yu-Ling
Huang, Kai-Fa
Lai, Hsin-Mei
Liao, Jiahn-Haur
Lee, Chai-Siah
Chang, Chiao-Min
Mak, Huey-Ming
Hsieh, Cheng-Wei
Lin, Chu-Chi
Melderen, Laurence Van
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 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.
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Type
journal article
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