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  • Title: Features of a twin-arginine signal peptide required for recognition by a Tat proofreading chaperone.
    Author: Buchanan G, Maillard J, Nabuurs SB, Richardson DJ, Palmer T, Sargent F.
    Journal: FEBS Lett; 2008 Dec 10; 582(29):3979-84. PubMed ID: 19013157.
    Abstract:
    The 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.
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