Pseudomonas Aerginosa Outer Membrane Carboxylate Channels Examined at the Single-Molecule Level Reveals Conserved Selectivity within each Subfamily

Abstract

with different (from 0 to 6) combinations of truncated and full-length sequences. Formation of concatemers was assessed by the use of singlemolecule photobleaching and protein cross-linking. Whole-cell recordings from concatenated PANX1 constructs suggest that at least four intact C-termini are required to inhibit channel activity. In addition, as the number of intact C-termini increased, there was a progressive decrease in single channel conductance, suggesting that individual C-termini may act within the multimeric channel to inhibit channel conductance. These results provide further mechanistic insights into the regulation of PANX1 channels by the C-terminal autoinhibitory domains.