TatBC, TatB, and TatC form structurally autonomous units within the twin arginine protein transport system of Escherichia coli

George L. Orriss, Michael J. Tarry, Berengere Ize, Frank Sargent, Susan M. Lea, Tracy Palmer, Ben C. Berks

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    43 Citations (Scopus)

    Abstract

    The Tat (twin arginine translocation) system transports folded proteins across bacterial and thylakoid membranes. The integral membrane proteins TatA, TatB, and TatC are the essential components of the Tat pathway in Escherichia coli. We demonstrate that formation of a stable complex between TatB and TatC does not require TatA or other Tat components. We show that the TatB and TatC proteins are each able to a form stable, defined, homomultimeric complexes. These we suggest correspond to structural subcomplexes within the parental TatBC complex. We infer that TatC forms a core to the TatBC complex on to which TatB assembles. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

    Original languageEnglish
    Pages (from-to)4091-4097
    Number of pages7
    JournalFEBS Letters
    Volume581
    Issue number21
    DOIs
    Publication statusPublished - 2007

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