Twin-Arginine Protein TranslocationGoosens, V. J. & van Dijl, J. M., 2017, Protein and Sugar Export and Assembly in Gram-positive Bacteria. Bagnoli, F. & Rappuoli, R. (eds.). SPRINGER-VERLAG BERLIN, Vol. 404. p. 69-94 26 p. (Current Topics in Microbiology and Immunology; vol. 404).
Research output: Chapter in Book/Report/Conference proceeding › Chapter › Academic
Twin-arginine protein translocation systems (Tat) translocate fully folded and co-factor-containing proteins across biological membranes. In this review, we focus on the Tat pathway of Gram-positive bacteria. The minimal Tat pathway is composed of two components, namely a TatA and TatC pair, which are often complemented with additional TatA-like proteins. We provide overviews of our current understanding of Tat pathway composition and mechanistic aspects related to Tat-dependent cargo protein translocation. This includes Tat pathway flexibility, requirements for the correct folding and incorporation of co-factors in cargo proteins and the functions of known cargo proteins. Tat pathways of several Gram-positive bacteria are discussed in detail, with emphasis on the Tat pathway of Bacillus subtilis. We discuss both shared and unique features of the different Gram-positive bacterial Tat pathways. Lastly, we highlight topics for future research on Tat, including the development of this protein transport pathway for the biotechnological secretion of high-value proteins and its potential applicability as an antimicrobial drug target in pathogens.
|Title of host publication||Protein and Sugar Export and Assembly in Gram-positive Bacteria|
|Editors||Fabio Bagnoli, Rino Rappuoli|
|Number of pages||26|
|Publication status||Published - 2017|
|Name||Current Topics in Microbiology and Immunology|
- BACTERIUM BACILLUS-SUBTILIS, COMPLETE GENOME SEQUENCE, SEC-INDEPENDENT PROTEIN, FOLDING QUALITY-CONTROL, WATER-SOLUBLE FRAGMENT, LEADER-BINDING PROTEIN, TAT SIGNAL PEPTIDES, IRON-SULFUR PROTEIN, RIESKE FE/S PROTEIN, ESCHERICHIA-COLI