Torsten H. Walther

TL;DR: Interestingly, the APH showed an unexpectedly slanted alignment in the protein, different from that of the isolated APH peptide, which implies that the amphiphilic region of TatA is not just a flexible attachment to the transmembrane anchor but might be able to form intra- or even intermolecular salt-bridges, which could play a key role in pore assembly.

TL;DR: 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" is proposed.

TL;DR: Transmembrane helix-helix interactions mediate the folding and assembly of membrane proteins, which contain local charge clusters that are important for folding and function, and which have to be compatible with a stable insertion into the bilayer via the translocon.

TL;DR: The design, high-yield expression, detergent-aided purification and lipid-reconstitution of five constructs of TatA(d), overcoming difficulties associated with the very different hydrophobicities and sizes of these membrane protein fragments are reported.

TL;DR: The transmembrane protein TatA is the pore forming unit of the twin-arginine translocase (Tat), which has the unique ability of transporting folded proteins across the cell membrane, to obtain insight in the translocation mechanism.