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The twin-arginine translocation (Tat) protein export system is present in the cytoplasmic membranes of most bacteria and archaea and has the highly unusual property of transporting fully folded proteins. The system must therefore provide a transmembrane pathway that is large enough to allow the passage of structured macromolecular substrates of different sizes but that maintains the impermeability of the membrane to ions. In the Gram-negative bacterium Escherichia coli, this complex task can be achieved by using only three small membrane proteins: TatA, TatB and TatC. In this Review, we summarize recent advances in our understanding of how this remarkable machine operates.

Original publication

DOI

10.1038/nrmicro2814

Type

Journal article

Journal

Nat Rev Microbiol

Publication Date

11/06/2012

Volume

10

Pages

483 - 496

Keywords

Cell Membrane, Escherichia coli, Escherichia coli Proteins, Gene Expression Regulation, Bacterial, Membrane Transport Proteins