Abstract
Colicins are folded protein toxins that face the formidable task of translocating across one or both of the Escherichia coli cell membranes in order to induce cell death. This translocation is achieved by parasitizing host proteins. There has been much recent progress in our understanding of the early stages of colicin entry, including the binding of outer-membrane nutrient transporters and porins and the subsequent recruitment of periplasmic and inner-membrane proteins that, together, trigger translocation. As well as providing insights into how these toxins enter cells, these studies have highlighted some surprising similarities in the modes of action of the systems that colicins subvert.
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Acknowledgements
Many thanks to N. Housden for help with figures 2 and 3, and to G. Thomas for helpful comments on the manuscript. My sincere thanks to all my colIaborators and to members of my laboratory, past and present, for their contributions to the colicin project. In particular, I thank R. James and G. Moore for introducing me to the world of colicin biology. I gratefully acknowledge funding for our work on colicins and Tol proteins from the Biotechnology and Biological Sciences Research Council of the UK and The Wellcome Trust.
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Kleanthous, C. Swimming against the tide: progress and challenges in our understanding of colicin translocation. Nat Rev Microbiol 8, 843–848 (2010). https://doi.org/10.1038/nrmicro2454
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DOI: https://doi.org/10.1038/nrmicro2454
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