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Folding and self-assembly of the TatA translocation pore based on a charge zipper mechanism.

Walther, Torsten H; Gottselig, Christina; Grage, Stephan L; Wolf, Moritz; Vargiu, Attilio V; Klein, Marco J; Vollmer, Stefanie; Prock, Sebastian; Hartmann, Mareike; Afonin, Sergiy; Stockwald, Eva; Heinzmann, Hartmut; Nolandt, Olga V; Wenzel, Wolfgang; Ruggerone, Paolo; Ulrich, Anne S.
Cell; 152(1-2): 316-26, 2013 Jan 17.
Artigo em Inglês | MEDLINE | ID: mdl-23332763
We propose a concept for the folding and self-assembly of the pore-forming TatA complex from the Twin-arginine translocase and of other membrane proteins based on electrostatic "charge zippers." Each subunit of TatA consists of a transmembrane segment, an amphiphilic helix (APH), and a C-terminal densely charged region (DCR). The sequence of charges in the DCR is complementary to the charge pattern on the APH, suggesting that the protein can be "zipped up" by a ladder of seven salt bridges. The length of the resulting hairpin matches the lipid bilayer thickness, hence a transmembrane pore could self-assemble via intra- and intermolecular salt bridges. The steric feasibility was rationalized by molecular dynamics simulations, and experimental evidence was obtained by monitoring the monomer-oligomer equilibrium of specific charge mutants. Similar "charge zippers" are proposed for other membrane-associated proteins, e.g., the biofilm-inducing peptide TisB, the human antimicrobial peptide dermcidin, and the pestiviral E(RNS) protein.
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