The Oligomeric State and Arrangement of the Active Bacterial Translocon*

@inproceedings{Deville2011TheOS,
  title={The Oligomeric State and Arrangement of the Active Bacterial Translocon*},
  author={Karine Deville and Vicki A. M. Gold and Alice Robson and Sarah Lilian Whitehouse and Richard B. Sessions and Stephen A. Baldwin and Sheena E Radford and Ian Collinson},
  booktitle={The Journal of biological chemistry},
  year={2011}
}
Protein secretion in bacteria is driven through the ubiquitous SecYEG complex by the ATPase SecA. The structure of SecYEG alone or as a complex with SecA in detergent reveal a monomeric heterotrimer enclosing a central protein channel, yet in membranes it is dimeric. We have addressed the functional significance of the oligomeric status of SecYEG in protein translocation using single molecule and ensemble methods. The results show that while monomers are sufficient for the SecA- and ATP… CONTINUE READING

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Advances in Membrane Proteins

Springer Singapore • 2018

Specific cardiolipin-SecY interactions are required for proton-motive force stimulation of protein secretion.

Proceedings of the National Academy of Sciences of the United States of America • 2018
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SecA—a New Twist in the Tale

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