Substrate-gated docking of pore subunit Tha4 in the TatC cavity initiates Tat translocase assembly

@inproceedings{Aldridge2014SubstrategatedDO,
  title={Substrate-gated docking of pore subunit Tha4 in the TatC cavity initiates Tat translocase assembly},
  author={Cassie Aldridge and Xianyue Ma and Fabien G{\'e}rard and Kenneth Cline},
  booktitle={The Journal of cell biology},
  year={2014}
}
The twin-arginine translocase (Tat) transports folded proteins across tightly sealed membranes. cpTatC is the core component of the thylakoid translocase and coordinates transport through interactions with the substrate signal peptide and other Tat components, notably the Tha4 pore-forming component. Here, Cys-Cys matching mapped Tha4 contact sites on cpTatC and assessed the role of signal peptide binding on Tha4 assembly with the cpTatC-Hcf106 receptor complex. Tha4 made contact with a… CONTINUE READING
Highly Cited
This paper has 17 citations. REVIEW CITATIONS

Citations

Publications citing this paper.
Showing 1-10 of 11 extracted citations

Mechanistic Aspects of Folded Protein Transport by the Twin Arginine Translocase (Tat).

The Journal of biological chemistry • 2015
View 21 Excerpts
Highly Influenced

The twin-arginine protein translocation pathway.

Annual review of biochemistry • 2015
View 10 Excerpts
Highly Influenced

1 Thylakoid-integrated recombinant Hcf 106 participates in the chloroplast Twin 1 Arginine Transport ( cpTat ) system 2 3

Qianqian Maa, Kristen Fiteb, Christopher Paul Newa, Carole Dabney-Smitha
2018
View 2 Excerpts
Method Support
Highly Influenced

Assembling the Tat protein translocase

View 5 Excerpts
Highly Influenced

References

Publications referenced by this paper.
Showing 1-10 of 33 references

Structure analysis of the membrane - bound PhoD signal peptide of the Tat translocase shows an N - terminal amphiphilic helix

B. C. Berks
Biochim . Biophys . Acta . • 2012
View 1 Excerpt