The twin-arginine protein translocation pathway.

@article{Berks2015TheTP,
  title={The twin-arginine protein translocation pathway.},
  author={Ben C. Berks},
  journal={Annual review of biochemistry},
  year={2015},
  volume={84},
  pages={
          843-64
        }
}
  • B. Berks
  • Published 2 June 2015
  • Biology
  • Annual review of biochemistry
The twin-arginine translocation (Tat) system, found in prokaryotes, chloroplasts, and some mitochondria, allows folded proteins to be moved across membranes. How this transport is achieved without significant ion leakage is an intriguing mechanistic question. Tat transport is mediated by complexes formed from small integral membrane proteins from just two protein families. Atomic-resolution structures have recently been determined for representatives of both these protein families, providing… 
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Mechanistic Aspects of Folded Protein Transport by the Twin Arginine Translocase (Tat)*
  • K. Cline
  • Biology
    The Journal of Biological Chemistry
  • 2015
The twin arginine translocase (Tat) transports folded proteins of widely varying size across ionically tight membranes with only 2–3 components of machinery and the proton motive force. Tat operates…
Targeting of proteins to the twin‐arginine translocation pathway
TLDR
This review will summarise recent advances in understanding of Tat transport, focusing in particular on the roles played by Tat signal peptides in protein targeting and translocation.
Precursor–Receptor Interactions in the Twin Arginine Protein Transport Pathway Probed with a New Receptor Complex Preparation
TLDR
The detergent glyco-diosgenin (GDN) can be used in place of digitonin to isolate homogeneous TatBC complexes that bind precursor proteins with physiological specificity and is used to quantitatively characterize TatBC–precursor interactions in a fully defined system.
Twin-Arginine Protein Translocation.
TLDR
This review provides overviews of the current understanding of Tat pathway composition and mechanistic aspects related to Tat-dependent cargo protein translocation, including Tat pathway flexibility, requirements for the correct folding and incorporation of co-factors in cargo proteins and the functions of known cargo proteins.
Assembling the Tat protein translocase
TLDR
This work combines sequence co-evolution analysis, molecular simulations, and experimentation to define the interactions between the Tat proteins of Escherichia coli at molecular-level resolution and finds that TatA also associates with TatC at the polar cluster site.
Twin-arginine translocase component TatB performs folding quality control via a general chaperone activity
TLDR
In vitro folding experiments revealed that the membrane-extrinsic domain of TatB possessed general chaperone activity, transiently binding to highly structured, partially unfolded intermediates of a model protein, citrate synthase, thereby preventing its irreversible aggregation and stabilizing the active species.
Hydrophobic mismatch effect is a key factor in protein transport on the Tat pathway
TLDR
A model of Tat transport utilizing localized toroidal pores that form when the membrane bilayer is thinned to a critical threshold is supported, seen as a compromise between the need for some hydrophobic mismatch to allow the membrane to reversibly reach the threshold thinness required for toroidal pore formation, and the permanently destabilizing effect of placing even shorter helices into these energy-transducing membranes.
A unifying mechanism for the biogenesis of prokaryotic membrane proteins co-operatively integrated by the Sec and Tat pathways
TLDR
It is shown that a combination of relatively low hydrophobicity of TMD3, coupled with the presence of C-terminal positively-charged amino acids, results in abortive insertion of T MD3 by the Sec pathway and its release at the cytoplasmic side of the membrane.
A signal sequence suppressor mutant that stabilizes an assembled state of the twin arginine translocase
TLDR
It is concluded that Tat signal peptides play roles in substrate targeting and in triggering assembly of the active translocase, even allowing transport of a Tat substrate lacking a signal peptide.
Probing the quality control mechanism of the Escherichia coli twin-arginine translocase with folding variants of a de novo–designed heme protein
TLDR
The clear correlation between the level of Tat-dependent export and the degree of heme b–induced folding of the maquette protein suggested that the membrane-bound Tat machinery can sense the extent of folding and conformational flexibility of its substrates.
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References

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TLDR
This Review summary summarizes recent advances in understanding of how the twin-arginine translocation protein export system operates in the cytoplasmic membranes of bacteria and archaea.
Structure of the TatC core of the twin-arginine protein transport system
TLDR
The crystal structure of TatC from the hyperthermophilic bacterium Aquifex aeolicus is reported, providing a molecular description of the core of the Tat translocation system and a framework for understanding the unique Tat transport mechanism.
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Structural model for the protein-translocating element of the twin-arginine transport system
TLDR
A structural model of the Escherichia coli TatA complex in detergent solution by NMR suggests that TatA facilitates protein transport by sensitizing the membrane to transient rupture, suggesting a mechanism of protein translocation involving thinning and perturbing the membrane bilayer.
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TLDR
An alternative model is presented which proposes that membrane integration could precede Tat-dependent translocation, and is mainly supported by the recent observations of Tat-independent membrane insertion of Tat substrates in vivo and in vitro.
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TLDR
This study demonstrates for the first time Tat transport for fully unstructured proteins, using signal sequence fusions to naturally unfolded FG repeats from the yeast Nsp1p nuclear pore protein, and explains the observed restriction of the Tat system to folded globular proteins on a molecular level.
The importance of the twin-arginine translocation pathway for bacterial virulence.
Solution structure of the TatB component of the twin-arginine translocation system.
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TLDR
It is shown that TatA can be purified independently of the other Tat proteins as a 460 kDa homooligomeric complex, which requires the amino-terminal membrane-anchoring domain of TatA.
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