A naturally occurring bacterial Tat signal peptide lacking one of the 'invariant' arginine residues of the consensus targeting motif

Andrew P. Hinsley, Nicola R. Stanley, Tracy Palmer, Ben C. Berks

    Research output: Contribution to journalArticlepeer-review

    94 Citations (Scopus)

    Abstract

    Currently described substrates of the bacterial Tat protein transport system are directed for export by signal peptides containing a pair of invariant arginine residues. The signal peptide of the TtrB subunit of Salmonella enterica tetrathionate reductase contains a single arginine residue but is nevertheless able to mediate Tat pathway transport. This naturally occurring example of a Tat signal peptide lacking a consensus arginine pair expands the range of sequences that can target a protein to the Tat pathway. The possible implications of this finding for the assembly of electron transfer complexes containing Rieske proteins in plant organelles are discussed.
    Original languageEnglish
    Pages (from-to)45-9
    Number of pages5
    JournalFEBS Letters
    Volume497
    Issue number1
    DOIs
    Publication statusPublished - 18 May 2001

    Keywords

    • Sec-independent
    • Bacterial protein export
    • Tat pathway
    • Twin-arginine signal peptide
    • Tetrathionate reductase
    • Rieske protein

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