| Autor: |
Colin Kleanthous, Nicholas G. Housden, Renata Kaminska, Sasha R. Derrington, David J. Brockwell, Sheena E. Radford, Oliver E. Farrance |
| Rok vydání: |
2014 |
| Předmět: |
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| Zdroj: |
Biophysical Journal. 106(2):385a-386a |
| ISSN: |
0006-3495 |
| DOI: |
10.1016/j.bpj.2013.11.2181 |
| Popis: |
Colicins are antimicrobial proteins produced by bacteria. Their highly active modes of killing make colicins of interest as a potential new class of antibiotics. However, the precise mechanism of cytotoxicity is not understood thus limiting their translation to biotechnological applications.It is thought that colicin intoxication occurs via a series of protein-protein interactions (PPIs) that span the periplasm (Housden et al. Science, 2013). Mechanical force may play a role in this process by an inside-out energy transduction mechanism. Periplasmic proteins that are subverted by colicins have either a known role in applying force during their normal function in-vivo or are highly homologous to proteins that do.In this work we study the colicin E9 system and the PPIs that remodel during its translocation across the outer and inner membranes of E. coli. Through a series of in-vitro single molecule force spectroscopy experiments performed using an atomic force microscope, we identify a mechanism by which dissociation of the highly avid colicin E9-immunity protein interaction (fM affinity, half-life days) can take place via the application of small forces ( |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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