A subset of bacterial inner membrane proteins integrated by the twin-arginine translocase

Kostas Hatzixanthis, Tracy Palmer, Frank Sargent

    Research output: Contribution to journalArticle

    96 Citations (Scopus)

    Abstract

    A group of bacterial exported proteins are synthesized with N-terminal signal peptides containing a SRRxFLK ‘twin-arginine’ amino acid motif. Proteins bearing twin-arginine signal peptides are targeted post-translationally to the twin-arginine translocation (Tat) system which transports folded substrates across the inner membrane. In Escherichia coli, most integral inner membrane proteins are assembled by a co-translational process directed by SRP/FtsY, the SecYEG translocase, and YidC. In this work we define a novel class of integral membrane proteins assembled by a Tat-dependent mechanism. We show that at least five E. coli Tat substrate proteins contain hydrophobic C-terminal transmembrane helices (or ‘C-tails’). Fusions between the identified transmembrane C-tails and the exclusively Tat-dependent reporter proteins TorA and SufI render the resultant chimeras membrane-bound. Export-linked signal peptide processing and membrane integration of the chimeras is shown to be both Tat-dependent and YidC-independent. It is proposed that the mechanism of membrane integration of proteins by the Tat system is fundamentally distinct from that employed for other bacterial inner membrane proteins.
    Original languageEnglish
    Pages (from-to)1377-1390
    Number of pages14
    JournalMolecular Microbiology
    Volume49
    Issue number5
    DOIs
    Publication statusPublished - 2003

    Fingerprint

    Arginine
    Membrane Proteins
    Protein Sorting Signals
    Membranes
    Escherichia coli
    Amino Acid Motifs
    Bacterial Proteins
    Protein Transport
    Proteins
    Twin-Arginine-Translocation System

    Keywords

    • Twin arginine signal peptide
    • Tat pathway
    • Protein transport
    • Bacterial transport

    Cite this

    Hatzixanthis, Kostas ; Palmer, Tracy ; Sargent, Frank. / A subset of bacterial inner membrane proteins integrated by the twin-arginine translocase. In: Molecular Microbiology. 2003 ; Vol. 49, No. 5. pp. 1377-1390.
    @article{d12cecf8360c4f08b718aec55354b952,
    title = "A subset of bacterial inner membrane proteins integrated by the twin-arginine translocase",
    abstract = "A group of bacterial exported proteins are synthesized with N-terminal signal peptides containing a SRRxFLK ‘twin-arginine’ amino acid motif. Proteins bearing twin-arginine signal peptides are targeted post-translationally to the twin-arginine translocation (Tat) system which transports folded substrates across the inner membrane. In Escherichia coli, most integral inner membrane proteins are assembled by a co-translational process directed by SRP/FtsY, the SecYEG translocase, and YidC. In this work we define a novel class of integral membrane proteins assembled by a Tat-dependent mechanism. We show that at least five E. coli Tat substrate proteins contain hydrophobic C-terminal transmembrane helices (or ‘C-tails’). Fusions between the identified transmembrane C-tails and the exclusively Tat-dependent reporter proteins TorA and SufI render the resultant chimeras membrane-bound. Export-linked signal peptide processing and membrane integration of the chimeras is shown to be both Tat-dependent and YidC-independent. It is proposed that the mechanism of membrane integration of proteins by the Tat system is fundamentally distinct from that employed for other bacterial inner membrane proteins.",
    keywords = "Twin arginine signal peptide, Tat pathway, Protein transport, Bacterial transport",
    author = "Kostas Hatzixanthis and Tracy Palmer and Frank Sargent",
    note = "dc.publisher: Wiley-Blackwell",
    year = "2003",
    doi = "10.1046/j.1365-2958.2003.03642.x",
    language = "English",
    volume = "49",
    pages = "1377--1390",
    journal = "Molecular Microbiology",
    issn = "0950-382X",
    publisher = "Wiley",
    number = "5",

    }

    A subset of bacterial inner membrane proteins integrated by the twin-arginine translocase. / Hatzixanthis, Kostas; Palmer, Tracy; Sargent, Frank.

    In: Molecular Microbiology, Vol. 49, No. 5, 2003, p. 1377-1390.

    Research output: Contribution to journalArticle

    TY - JOUR

    T1 - A subset of bacterial inner membrane proteins integrated by the twin-arginine translocase

    AU - Hatzixanthis, Kostas

    AU - Palmer, Tracy

    AU - Sargent, Frank

    N1 - dc.publisher: Wiley-Blackwell

    PY - 2003

    Y1 - 2003

    N2 - A group of bacterial exported proteins are synthesized with N-terminal signal peptides containing a SRRxFLK ‘twin-arginine’ amino acid motif. Proteins bearing twin-arginine signal peptides are targeted post-translationally to the twin-arginine translocation (Tat) system which transports folded substrates across the inner membrane. In Escherichia coli, most integral inner membrane proteins are assembled by a co-translational process directed by SRP/FtsY, the SecYEG translocase, and YidC. In this work we define a novel class of integral membrane proteins assembled by a Tat-dependent mechanism. We show that at least five E. coli Tat substrate proteins contain hydrophobic C-terminal transmembrane helices (or ‘C-tails’). Fusions between the identified transmembrane C-tails and the exclusively Tat-dependent reporter proteins TorA and SufI render the resultant chimeras membrane-bound. Export-linked signal peptide processing and membrane integration of the chimeras is shown to be both Tat-dependent and YidC-independent. It is proposed that the mechanism of membrane integration of proteins by the Tat system is fundamentally distinct from that employed for other bacterial inner membrane proteins.

    AB - A group of bacterial exported proteins are synthesized with N-terminal signal peptides containing a SRRxFLK ‘twin-arginine’ amino acid motif. Proteins bearing twin-arginine signal peptides are targeted post-translationally to the twin-arginine translocation (Tat) system which transports folded substrates across the inner membrane. In Escherichia coli, most integral inner membrane proteins are assembled by a co-translational process directed by SRP/FtsY, the SecYEG translocase, and YidC. In this work we define a novel class of integral membrane proteins assembled by a Tat-dependent mechanism. We show that at least five E. coli Tat substrate proteins contain hydrophobic C-terminal transmembrane helices (or ‘C-tails’). Fusions between the identified transmembrane C-tails and the exclusively Tat-dependent reporter proteins TorA and SufI render the resultant chimeras membrane-bound. Export-linked signal peptide processing and membrane integration of the chimeras is shown to be both Tat-dependent and YidC-independent. It is proposed that the mechanism of membrane integration of proteins by the Tat system is fundamentally distinct from that employed for other bacterial inner membrane proteins.

    KW - Twin arginine signal peptide

    KW - Tat pathway

    KW - Protein transport

    KW - Bacterial transport

    U2 - 10.1046/j.1365-2958.2003.03642.x

    DO - 10.1046/j.1365-2958.2003.03642.x

    M3 - Article

    VL - 49

    SP - 1377

    EP - 1390

    JO - Molecular Microbiology

    JF - Molecular Microbiology

    SN - 0950-382X

    IS - 5

    ER -