The Tat Substrate CueO Is Transported in an Incomplete Folding State.

@article{Stolle2016TheTS,
  title={The Tat Substrate CueO Is Transported in an Incomplete Folding State.},
  author={Patrick Stolle and Bo Hou and Thomas Br{\"u}ser},
  journal={The Journal of biological chemistry},
  year={2016},
  volume={291 26},
  pages={13520-8}
}
In Escherichia coli, cytoplasmic copper ions are toxic to cells even at the lowest concentrations. As a defense strategy, the cuprous oxidase CueO is secreted into the periplasm to oxidize the more membrane-permeable and toxic Cu(I) before it can enter the cytoplasm. CueO itself is a multicopper oxidase that requires copper for activity. Because it is transported by the twin-arginine translocation (Tat) pathway, which transports folded proteins, a requirement for cofactor assembly before… CONTINUE READING

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