Characterisation of the membrane-extrinsic domain of the TatB component of the twin arginine protein translocase

Barbara Maldonado , Holger Kneuper, Grant Buchanan, Kostas Hatzixanthis, Frank Sargent, Ben C. Berks, Tracy Palmer

    Research output: Contribution to journalArticle

    14 Citations (Scopus)

    Abstract

    The twin arginine protein transport (Tat) system transports folded proteins across cytoplasmic membranes of bacteria and thylakoid membranes of plants, and in Escherichia coli it comprises TatA, TatB and TatC components. In this study we show that the membrane extrinsic domain of TatB forms parallel contacts with at least one other TatB protein. Truncation of the C-terminal two thirds of TatB still allows complex formation with TatC, although protein transport is severely compromised. We were unable to isolate transport-inactive single codon substitution mutations in tatB suggesting that the precise amino acid sequence of TatB is not critical to its function.

    Structured summary:

    TatA physically interacts with TatA by two hybrid (View interaction)

    TatB and TatC bind by molecular sieving (View interaction)

    TatB physically interacts with TatB by two hybrid (View Interaction 1, 2) (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

    Original languageEnglish
    Pages (from-to)478-484
    Number of pages7
    JournalFEBS Letters
    Volume585
    Issue number3
    DOIs
    Publication statusPublished - 4 Feb 2011

    Keywords

    • Protein transport
    • Twin arginine signal peptide
    • Tat pathway
    • TatB
    • Protein:protein interaction
    • Mutagenesis
    • SEC-INDEPENDENT PROTEIN
    • CYSTEINE-SCANNING MUTAGENESIS
    • BACTERIAL 2-HYBRID SYSTEM
    • ESCHERICHIA-COLI
    • TRANSPORT SYSTEM
    • SIGNAL PEPTIDE
    • EXPORT PATHWAY
    • BINDING
    • COMPLEXES
    • RESIDUES

    Cite this