Journal
CELL
Volume 152, Issue 1-2, Pages 316-326Publisher
CELL PRESS
DOI: 10.1016/j.cell.2012.12.017
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Funding
- YIG grant (KIT Karlsruhe, Germany)
- HPC Programme of the BW Stiftung
- Regione Autonoma della Sardegna through a Research Fellow on fundings PO Sardegna FSE Promozione della ricerca scientifica e dell'innovazione tecnologica in Sardegna [L.R.7/2007]
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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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