The entire N-terminal half of TatC is involved in twin-arginine precursor binding

Eva Holzapfel, Gottfried Eisner, Meriem Alami, Claire M. L. Barrett, Grant Buchanan, Iris Lueke, Jean-Michel Betton, Colin Robinson, Tracy Palmer, Michael Moser, Matthias Mueller

    Research output: Contribution to journalArticlepeer-review

    63 Citations (Scopus)


    Translocation of twin-arginine precursor proteins across the cytoplasmic membrane of Escherichia coli requires the three membrane proteins TatA, TatB, and TatC. TatC and TatB were shown to be involved in precursor binding. We have analyzed in vitro a number of single alanine substitutions in tatC that were previously shown to compromise in vivo the function of the Tat translocase. All tatC mutants that were defective in precursor translocation into cytoplasmic membrane vesicles concomitantly interfered with precursor binding not only to TatC but also to TatB. Hence structural changes of TatC that affect precursor targeting simultaneously abolish engagement of the twin-arginine signal sequence with TatB and block the formation of a functional Tat translocase. Since these phenotypes were observed for tatC mutations spread over the first half of TatC, this entire part of the molecule must globally be involved in precursor binding.

    Original languageEnglish
    Pages (from-to)2892-2898
    Number of pages7
    Issue number10
    Publication statusPublished - 2007


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