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Energetic and Spatial Parameters for Gating of the Bacterial Large Conductance Mechanosensitive Channel, MscL
The tension dependence of channel gating is primarily one of increasing the external channel area to accommodate the pore of the smallest conducting state and the in-plane area change from closed to fully open was 6 nm2, agreeing with the value obtained in the two-state analysis. Expand
Structural models of the MscL gating mechanism.
The proposed gating mechanism reveals critical spatial relationships between the expandable transmembrane barrel formed by M1 and M2, the gate formed by S1 helices, and "strings" that link S1s to M1s. Expand
The gating mechanism of the large mechanosensitive channel MscL
Structural models in which a cytoplasmic gate is formed by a bundle of five amino-terminal helices (S1), previously unresolved in the crystal structure, are developed, revealing critical spatial relationships between the domains that transmit force from the lipid bilayer to the channel gate. Expand
A large-conductance mechanosensitive channel in E. coli encoded by mscL alone
The mscL nucleotide sequence predicts a unique protein of only 136 amino acids, with a highly hydrophobic core and very different from porins or other known proteins. Expand
Purification of the small mechanosensitive channel of Escherichia coli (MscS): the subunit structure, conduction, and gating characteristics in liposomes.
  • S. Sukharev
  • Chemistry, Medicine
  • Biophysical journal
  • 1 July 2002
It is shown that that the isolated 31-kDa MscS protein is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer, and the correspondence between channel properties in the native and reconstituted systems is discussed. Expand
Single residue substitutions that change the gating properties of a mechanosensitive channel in Escherichia coli.
It is shown that a short deletion from the amino terminus (3 amino acids), and a larger deletion of 27 amino acids from the carboxyl terminus of this protein, had little if any effect in channel properties, and narrowed the search of the core mechanosensitive mechanism to 106 residues of this 136-amino acid protein. Expand
Membrane topology and multimeric structure of a mechanosensitive channel protein of Escherichia coli.
Cross‐linking studies suggest that the functional MscL complex is a homohexamer, consistent with a protein domain assignment and topological model which is proposed and discussed. Expand
Mechanosensitive channels of Escherichia coli: the MscL gene, protein, and activities.
A 2.5-ns mechanosensitive conductance in giant E. coli spheroplasts is discovered and several residues, which when deleted or substituted, affect channel kinetics or mechanosensitivity are identified. Expand
Water dynamics and dewetting transitions in the small mechanosensitive channel MscS.
It is inferred that MscS gate, which is similar to that of the nicotinic ACh receptor, involves a vapor-lock mechanism where limited changes of geometry or surface polarity can locally switch the regime between water-filled (conducting) and empty (non Conducting) states. Expand
Electroporation and electrophoretic DNA transfer into cells. The effect of DNA interaction with electropores.
The data suggest that the mechanism of cell electrotransfection is underlain by electrophoretic movement of DNA through membrane pores, the size of which is determined by interaction with DNA in an electric field. Expand