The twin-arginine transport system: moving folded proteins across membranes

F. Sargent

    Research output: Contribution to journalArticlepeer-review

    91 Citations (Scopus)

    Abstract

    The Tat (twin-arginine transport) pathway is a protein-targeting system dedicated to the transmembrane translocation of fully folded proteins. This system is highly prevalent in the cytoplasmic membranes of bacteria and archaea, and is also found in the thylakoid membranes of plant chloroplasts and possibly also in the inner membrane of plant mitochondria. Proteins are targeted to a membrane-embedded Tat translocase by specialized N-terminal twin-arginine signal peptides bearing an SRRXFLK amino acid motif. The genes encoding components of the Tat translocase were discovered approx. 10 years ago, and, since then, research in this area has expanded on a global scale. in this review, the key discoveries in this field are summarized, and recent studies of bacterial twin-arginine signal-peptide-binding proteins are discussed.

    Original languageEnglish
    Pages (from-to)835-847
    Number of pages13
    JournalBiochemical Society Transactions
    Volume35
    Issue number5
    DOIs
    Publication statusPublished - Nov 2007

    Keywords

    • membrane protein
    • membrane transport
    • molecular chaperone
    • protein-protein interaction
    • protein targeting
    • twin-arginine translocase
    • DIMETHYL-SULFOXIDE REDUCTASE
    • SIGNAL PEPTIDE-BINDING
    • PERIPLASMIC NITRATE REDUCTASE
    • SEC-INDEPENDENT PROTEIN
    • FAMILY INTRAMEMBRANE PROTEASE
    • CYSTEINE-SCANNING MUTAGENESIS
    • TRANSLOCASE TATC COMPONENT
    • GREEN FLUORESCENT PROTEIN
    • FOLDING QUALITY-CONTROL
    • ESCHERICHIA-COLI K-12

    Cite this