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

  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},
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
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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
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