Abstract
The Tat (twin arginine translocation) system is a recently discovered protein transport pathway which is found in the cytoplasmic membranes of many bacteria, and in the energy-transducing membranes of plant organelles. Proteins are targeted to the Tat export machinery by N-terminal signal peptides harbouring a distinctive ‘twin arginine’ motif. The Tat system serves to export a subset of periplasmic and periplasmic-facing proteins that normally require redox cofactors for activity. Overwhelming evidence suggests that substrate proteins are translocated across the membrane in a folded conformation, with their redox cofactors already bound, and in some cases as hetero-oligomers. This remarkable translocase is the first example of a protein transport system transporting folded substrates across an energy-coupling membrane. Here, the salient features of the bacterial Tat protein export pathway are discussed.
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Palmer, T., Berks, B.C. (2003). The Tat Protein Export Pathway. In: Oudega, B. (eds) Protein Secretion Pathways in Bacteria. Springer, Dordrecht. https://doi.org/10.1007/978-94-010-0095-6_3
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DOI: https://doi.org/10.1007/978-94-010-0095-6_3
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