System-specific chaperones on the Tat protein transport pathway

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The twin-arginine protein transport (Tat) system is a remarkable molecular machine dedicated to the translocation of fully folded proteins across energy-transducing membranes. Cofactor-containing Tat substrates such as trimethylamine N-oxide reductase acquire their cofactors prior to export and substrate proteins actually require to be folded before transport can proceed. Thus it is very likely that mechanisms exist to prevent wasteful export of immature Tat substrates or curb competition between immature and mature substrates for the transporter. Using the model prokaryote Escherichia coli and the TorD molecular chaperone system, we will define the proofreading activity on the Tat pathway at the molecular and cellular levels.