The Tat protein export pathway

Authors

  • Ben C. Berks,

    1. Centre for Metalloprotein Spectroscopy and Biology, School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK.,
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  • Frank Sargent,

    1. Centre for Metalloprotein Spectroscopy and Biology, School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK.,
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  • Tracy Palmer

    1. Centre for Metalloprotein Spectroscopy and Biology, School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK.,
    2. Department of Molecular Microbiology, John Innes Centre, Colney, Norwich NR4 7UH, UK.
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Ben C. Berks. E-mail b.berks@uea.ac.uk; Tel. (+44) 1603 592186; Fax (+44) 1603 592250. E-mail Tracy.Palmer@bbsrc.ac.uk; Tel. (+44) 1603 456900; Fax (+44) 1603 454970.

Abstract

The Tat (twin-arginine translocation) system is a bacterial protein export pathway with the remarkable ability to transport folded proteins across the cytoplasmic membrane. Preproteins are directed to the Tat pathway by signal peptides that bear a characteristic sequence motif, which includes consecutive arginine residues. Here, we review recent progress on the characterization of the Tat system and critically discuss the structure and operation of this major new bacterial protein export pathway.

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