The role of MscL amphipathic N terminus indicates a blueprint for bilayer-mediated gating of mechanosensitive channels

Navid Bavi, D. Marien Cortes, Charles D. Cox, Paul R. Rohde, Weihong Liu, Joachim W. Deitmer, Omid Bavi, Pavel Strop, Adam P. Hill, Douglas Rees, Ben Corry, Eduardo Perozo () and Boris Martinac ()
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Navid Bavi: Victor Chang Cardiac Research Institute
D. Marien Cortes: Institute for Biophysical Dynamics, University of Chicago
Charles D. Cox: Victor Chang Cardiac Research Institute
Paul R. Rohde: Victor Chang Cardiac Research Institute
Weihong Liu: University of Western Australia
Joachim W. Deitmer: FB Biologie, University of Kaiserslautern
Omid Bavi: Victor Chang Cardiac Research Institute
Pavel Strop: Howard Hughes Medical Institute, California Institute of Technology
Adam P. Hill: Victor Chang Cardiac Research Institute
Douglas Rees: Howard Hughes Medical Institute, California Institute of Technology
Ben Corry: Research School of Biology, The Australian National University
Eduardo Perozo: Institute for Biophysical Dynamics, University of Chicago
Boris Martinac: Victor Chang Cardiac Research Institute

Nature Communications, 2016, vol. 7, issue 1, 1-13

Abstract: Abstract The bacterial mechanosensitive channel MscL gates in response to membrane tension as a result of mechanical force transmitted directly to the channel from the lipid bilayer. MscL represents an excellent model system to study the basic biophysical principles of mechanosensory transduction. However, understanding of the essential structural components that transduce bilayer tension into channel gating remains incomplete. Here using multiple experimental and computational approaches, we demonstrate that the amphipathic N-terminal helix of MscL acts as a crucial structural element during tension-induced gating, both stabilizing the closed state and coupling the channel to the membrane. We propose that this may also represent a common principle in the gating cycle of unrelated mechanosensitive ion channels, allowing the coupling of channel conformation to membrane dynamics.

Date: 2016
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DOI: 10.1038/ncomms11984

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