The Escherichia coli twin-arginine translocase: conserved residues of TatA and TatB family components involved in protein transport

Matthew G Hicks, Erik de Leeuw, Ida Porcelli, Grant Buchanan, Ben C Berks, Tracy Palmer

    Research output: Contribution to journalArticlepeer-review

    55 Citations (Scopus)


    The Escherichia coli Tat system serves to export folded proteins harbouring an N-terminal twin-arginine signal peptide across the cytoplasmic membrane. In this report we have studied the functions of conserved residues within the structurally related TatA and TatB proteins. Our results demonstrate that there are two regions within each protein of high sequence conservation that are critical for efficient Tat translocase function. The first region is the interdomain hinge between the transmembrane and the amphipathic alpha-helices of TatA and TatB proteins. The second region is within the amphipathic helices of TatA and TatB. In particular an invariant phenylalanine residue within TatA proteins is essential for activity, whereas a string of glutamic acid residues on the same face of the amphipathic helix of TatB; is important for function. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

    Original languageEnglish
    Pages (from-to)61-67
    Number of pages7
    JournalFEBS Letters
    Issue number1-3
    Publication statusPublished - 27 Mar 2003

    Cite this