Buchanan, GrantMaillard, JulienNabuurs, Sander BRichardson, David JPalmer, TracySargent, Frank2009-04-012009-04-012009-04-01200810.1016/j.febslet.2008.10.049https://infoscience.epfl.ch/handle/20.500.14299/36478The twin-arginine translocation (Tat) system is a bacterial protein targeting pathway. Tat-targeted proteins display signal peptides containing a distinctive SRRxFLK ‘twin-arginine’ motif. The Escherichia coli trimethylamine N-oxide reductase (TorA) bears a bifunctional Tat signal peptide, which directs protein export and serves as a binding site for the TorD biosynthetic chaperone. Here, the physical interaction between TorD and the TorA signal peptide was investigated. A single substitution within the TorA signal peptide (L31Q) was sufficient to impair TorD binding. Screening of a random torD mutant library identified a variant TorD protein (Q7L) that displayed increased binding affinity for the TorA signal peptide.Bacterial respirationBacterial protein targetingTwin-arginine signal peptideTat proofreading chaperoneProtein–protein interactionSite-directed mutagenesistext::journal::journal article::research article