title: Gating the bacterial mechanosensitive channels: MscS a new paradigm?
abstract: Mechanosensitive channels play major roles in protecting bacteria from hypo-osmotic shock. In the millisecond timescale they must achieve the transition from tightly closed oligomers to large, relatively non-discriminating pores. The crystal structure for MscL, combined with genetic and biochemical analysis, provided the initial insights for the mechanism by which this structural transition might be made. Discovery of the gene for a second class of mechanosensitive channel, MscS, and its subsequent crystallisation, has provided a new paradigm for mechanosensation, enabling a deeper understanding of the mechanisms of sensing membrane tension.
authors.affiliation: School of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, Scotland, UK. m.d.edwards@abdn.ac.uk
authors.forename: Michelle D
authors.initials: MD
authors.lastname: Edwards
authors.forename: Ian R
authors.initials: IR
authors.lastname: Booth
authors.forename: Samantha
authors.initials: S
authors.lastname: Miller
mesh_terms: D004926:Escherichia coli / Q000502:physiology*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000502:physiology*; D015640:Ion Channel Gating / Q000502:physiology; D007473:Ion Channels / Q000737:chemistry / Q000502:physiology*; D040542:Mechanotransduction, Cellular / Q000502:physiology*
chemical_list: D029968:Escherichia coli Proteins; D007473:Ion Channels; C086596:MscL protein, E coli; C469542:MscS protein, E coli