Transport of Folded Proteins by the Tat SystemFrain, K. M., Robinson, C. & van Dijl, J. M., Aug-2019, In : Protein journal. 38, 4, p. 377-388 12 p.
Research output: Contribution to journal › Review article › Academic › peer-review
The twin-arginine protein translocation (Tat) system has been characterized in bacteria, archaea and the chloroplast thylakoidal membrane. This system is distinct from other protein transport systems with respect to two key features. Firstly, it accepts cargo proteins with an N-terminal signal peptide that carries the canonical twin-arginine motif, which is essential for transport. Second, the Tat system only accepts and translocates fully folded cargo proteins across the respective membrane. Here, we review the core essential features of folded protein transport via the bacterial Tat system, using the three-component TatABC system of Escherichia coli and the two-component TatAC systems of Bacillus subtilis as the main examples. In particular, we address features of twin-arginine signal peptides, the essential Tat components and how they assemble into different complexes, mechanistic features and energetics of Tat-dependent protein translocation, cytoplasmic chaperoning of Tat cargo proteins, and the remarkable proofreading capabilities of the Tat system. In doing so, we present the current state of our understanding of Tat-dependent protein translocation across biological membranes, which may serve as a lead for future investigations.
|Number of pages||12|
|Publication status||Published - Aug-2019|
- TatA, TatB, TatC, Twin-arginine, Bacillus subtilis, Escherichia coli, TWIN-ARGININE TRANSLOCASE, SEC-INDEPENDENT PROTEIN, ESCHERICHIA-COLI TATA, CYSTEINE-SCANNING MUTAGENESIS, FOLDING QUALITY-CONTROL, BACILLUS-SUBTILIS, SIGNAL PEPTIDE, PROTON GRADIENT, DIFFERENTIAL INTERACTIONS, BACTERIAL PROTEINS