Features of a twin-arginine signal peptide required for recognition by a Tat proofreading chaperone

Grant Buchanan, Julien Maillard, Sander B. Nabuurs, David J. Richardson, Tracy Palmer, Frank Sargent

    Research output: Contribution to journalArticle

    28 Citations (Scopus)

    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.

    Original languageEnglish
    Pages (from-to)3979-3984
    Number of pages6
    JournalFEBS Letters
    Volume582
    Issue number29
    DOIs
    Publication statusPublished - 10 Dec 2008

    Keywords

    • Bacterial respiration
    • Bacterial protein targeting
    • Twin-arginine signal peptide
    • Tat proofreading chaperone
    • Protein-protein interaction
    • Site-directed mutagenesis
    • PROTEIN TRANSLOCATION PATHWAY
    • N-OXIDE REDUCTASE
    • ESCHERICHIA-COLI
    • DIRECTED MUTAGENESIS
    • EXPORT PATHWAY
    • TORD
    • MATURATION
    • MOLYBDOENZYME
    • INVOLVEMENT
    • BINDING

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