Membrane protein insertion and proton-motive-force-dependent secretion through the bacterial holo-translocon SecYEG-SecDF-YajC-YidC.

@article{Schulze2014MembranePI,
  title={Membrane protein insertion and proton-motive-force-dependent secretion through the bacterial holo-translocon SecYEG-SecDF-YajC-YidC.},
  author={Ryan J. Schulze and Joanna Komar and Mathieu Botte and William John Allen and Sarah L. Whitehouse and Vicki A. M. Gold and Jelger A. Lycklama a Nijeholt and Karine Huard and Imre Berger and Christiane Schaffitzel and Ian Collinson},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2014},
  volume={111 13},
  pages={
          4844-9
        }
}
The SecY/61 complex forms the protein-channel component of the ubiquitous protein secretion and membrane protein insertion apparatus. The bacterial version SecYEG interacts with the highly conserved YidC and SecDF-YajC subcomplex, which facilitates translocation into and across the membrane. Together, they form the holo-translocon (HTL), which we have successfully overexpressed and purified. In contrast to the homo-dimeric SecYEG, the HTL is a hetero-dimer composed of single copies of SecYEG… CONTINUE READING

Citations

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Unlocking the Bacterial SecY Translocon.

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Targeting and Insertion of Membrane Proteins.

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Optimizing membrane and secretory protein production in Gram-negative bacteria

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Dynamic interaction of the sec translocon with the chaperone PpiD.

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