Energetics of gating MscS by membrane tension in azolectin liposomes and giant spheroplasts.
Mechanosensitive (MS) ion channels are molecular sensors that detect and transduce signals across prokaryotic and eukaryotic cell membranes arising from external mechanical stimuli or osmotic gradients. They play an integral role in mechanosensory responses including touch, hearing, and proprioception by opening or closing in order to facilitate or prevent the flow of ions and organic osmolytes. In this study we use a linear force model of MS channel gating to determine the gating membrane tension (γ) and the gating area change (ΔA) associated with the energetics of MscS channel gating in giant spheroplasts and azolectin liposomes. Analysis of Boltzmann distribution functions describing the dependence of MscS channel gating on membrane tension indicated that the gating area change (ΔA) was the same for MscS channels recorded in both preparations. The comparison of the membrane tension (γ) gating the channel, however, showed a significant difference between the MscS channel activities in these two preparations.
Shaista
S
Shaikh
Charles D
CD
Cox
Takeshi
T
Nomura
Boris
B
Martinac
D018360:Crystallography, X-Ray; D004734:Energy Metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism*; D015640:Ion Channel Gating; D007473:Ion Channels / Q000737:chemistry / Q000378:metabolism*; D008081:Liposomes / Q000737:chemistry*; D018408:Patch-Clamp Techniques; D010713:Phosphatidylcholines / Q000494:pharmacology*; D017434:Protein Structure, Tertiary; D013104:Spheroplasts / Q000737:chemistry* / Q000187:drug effects
D029968:Escherichia coli Proteins; D007473:Ion Channels; D008081:Liposomes; C469542:MscS protein, E coli; D010713:Phosphatidylcholines; C024990:asolectin