Oligomeric properties and signal peptide binding by Escherichia coli Tat protein transport complexes

Erik de Leeuw, Thierry Granjon, Ida Porcelli, Meriem Alami, Stephen B Carr, Matthias Muller, Frank Sargent, Tracy Palmer, Ben C Berks

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    Abstract

    The Escherichia coli Tat apparatus is a protein translocation system that serves to export folded proteins across the inner membrane. The integral membrane proteins TatA, TatB and TatC are essential components of this pathway. Substrate proteins are directed to the Tat apparatus by specialized N-terminal signal peptides bearing a consensus twin-arginine sequence motif. Here we have systematically examined the Tat complexes that can be purified from overproducing strains. Our data suggest that the TatA, TatB and TatC proteins are found in at least two major types of high molecular mass complex in detergent solution, one consisting predominantly of TatA but with a small quantity of TatB, and the other based on a TatBC unit but also containing some TatA protein. The latter complex is shown to be capable of binding a Tat signal peptide. Using an alternative purification strategy we show that it is possible to isolate a TatABC complex containing a high molar excess of the TatA component. (C) 2002 Elsevier Science Ltd. All rights reserved.

    Original languageEnglish
    Pages (from-to)1135-1146
    Number of pages12
    JournalJournal of Molecular Biology
    Volume322
    Issue number5
    DOIs
    Publication statusPublished - 4 Oct 2002

    Cite this

    de Leeuw, E., Granjon, T., Porcelli, I., Alami, M., Carr, S. B., Muller, M., Sargent, F., Palmer, T., & Berks, B. C. (2002). Oligomeric properties and signal peptide binding by Escherichia coli Tat protein transport complexes. Journal of Molecular Biology, 322(5), 1135-1146. https://doi.org/10.1016/S0022-2836(02)00820-3