<i>In situ</i>, Reversible Gating of a Mechanosensitive Ion Channel through Protein-Lipid Interactions.

ABSTRACT: Understanding the functioning of ion channels, as well as utilizing their properties for biochemical applications requires control over channel activity. Herein we report a reversible control over the functioning of a mechanosensitive ion channel by interfering with its interaction with the lipid bilayer. The mechanosensitive channel of large conductance from Escherichia coli is reconstituted into liposomes and activated to its different sub-open states by titrating lysophosphatidylcholine (LPC) into the lipid bilayer. Activated channels are closed back by the removal of LPC out of the membrane by bovine serum albumin (BSA). Electron paramagnetic resonance spectra showed the LPC-dose-dependent gradual opening of the channel pore in the form of incrementally increasing spin label mob

SUBMITTER: Dimitrova A 

PROVIDER: S-EPMC5030285 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature