Abstract
The twin‐arginine protein transport (Tat pathway) is found in prokaryotes and plant organelles and transports folded proteins across membranes. Targeting of substrates to the Tat system is mediated by the presence of an N‐terminal signal sequence containing a highly conserved twin‐arginine motif. The Tat machinery comprises membrane proteins from the TatA and TatC families. Assembly of the Tat translocon is dynamic and is triggered by the interaction of a Tat substrate with the Tat receptor complex. This review will summarise recent advances in our understanding of Tat transport, focusing in particular on the roles played by Tat signal peptides in protein targeting and translocation.
Highlights
The general secretory (Sec) and twin-arginine translocation (Tat) pathways operate in parallel to transport proteins across the cytoplasmic membrane
The transport of proteins across lipid membranes is an essential biological process
Current evidence points to a model whereby the active Tat translocon assembles ‘on demand’ upon interaction with a substrate protein and that it disassembles once translocation is complete (Alami et al, 2003; Alcock et al, 2013; Mori & Cline, 2002; Rose, Fröbel, Graumann, & Müller, 2013; Figure 4)
Summary
The general secretory (Sec) and twin-arginine translocation (Tat) pathways operate in parallel to transport proteins across the cytoplasmic membrane. Current evidence points to a model whereby the active Tat translocon assembles ‘on demand’ upon interaction with a substrate protein and that it disassembles once translocation is complete (Alami et al, 2003; Alcock et al, 2013; Mori & Cline, 2002; Rose, Fröbel, Graumann, & Müller, 2013; Figure 4).
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