A force-activated trip switch triggers rapid dissociation of a colicin from its immunity protein.
| Autor: | Oliver E Farrance, Eleanore Hann, Renata Kaminska, Nicholas G Housden, Sasha R Derrington, Colin Kleanthous, Sheena E Radford, David J Brockwell |
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| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: | |
| Zdroj: | PLoS Biology, Vol 11, Iss 2, p e1001489 (2013) |
| Druh dokumentu: | article |
| ISSN: | 1544-9173 1545-7885 |
| DOI: | 10.1371/journal.pbio.1001489 |
| Popis: | Colicins are protein antibiotics synthesised by Escherichia coli strains to target and kill related bacteria. To prevent host suicide, colicins are inactivated by binding to immunity proteins. Despite their high avidity (K(d) ≈ fM, lifetime ≈ 4 days), immunity protein release is a pre-requisite of colicin intoxication, which occurs on a timescale of minutes. Here, by measuring the dynamic force spectrum of the dissociation of the DNase domain of colicin E9 (E9) and immunity protein 9 (Im9) complex using an atomic force microscope we show that application of low forces ( |
| Databáze: | Directory of Open Access Journals |
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