Investigating the molecular mechanisms of colicin import into Escherichia coli cells
Aleanizy, Fadilah (2012) Investigating the molecular mechanisms of colicin import into Escherichia coli cells. PhD thesis, University of Nottingham.
Colicins are a family of bacterial toxins, which kill Escherichia coli cells and other closely related species. Their mode of action requires binding to an outer membrane receptor, translocation across the cell envelope leading to cytotoxicity at specific targets. The mechanism of colicin cytotoxicity includes a non-specific endonuclease activity or depolarizing of the cytoplasmic membrane by pore-forming activity. The cytotoxic activity can be inhibited by the high affinity binding of an immunity protein. For Group A colicins, translocation requires interaction between the N-terminal domain of the colicin and a series of membrane bound and periplasmic proteins called the Tol system (TolB, TolR, TolA, TolQ and Pal). In order to allow cytotoxicity, the immunity protein of enzymatic colicins must be lost after binding of the colicin to a target cell and the cytotoxic domain has to be translocated through both the outer and inner membranes.
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