Targeting of proteins to the twin-arginine translocation pathway

Mol Microbiol. 2020 May;113(5):861-871. doi: 10.1111/mmi.14461. Epub 2020 Feb 20.

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.

Keywords: Tat pathway; folded protein; mechanism; protein transport; twin-arginine signal peptide.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Motifs*
  • Bacterial Proteins / physiology
  • Cell Membrane
  • Escherichia coli Proteins / physiology
  • Membrane Transport Proteins / physiology
  • Protein Binding
  • Protein Conformation
  • Protein Sorting Signals*
  • Protein Transport*
  • Twin-Arginine-Translocation System / physiology*

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • Membrane Transport Proteins
  • Protein Sorting Signals
  • Twin-Arginine-Translocation System
  • twin-arginine translocase complex, E coli