Interaction of the colicin K bactericidal toxin with components of its import machinery in the periplasm of Escherichia coli.

ABSTRACT: Colicins are bacterial antibiotic toxins produced by Escherichia coli cells and are active against E. coli and closely related strains. To penetrate the target cell, colicins bind to an outer membrane receptor at the cell surface and then translocate their N-terminal domain through the outer membrane and the periplasm. Once fully translocated, the N-terminal domain triggers entry of the catalytic C-terminal domain by an unknown process. Colicin K uses the Tsx nucleoside-specific receptor for binding at the cell surface, the OmpA protein for translocation through the outer membrane, and the TolABQR proteins for the transit through the periplasm. Here, we initiated studies to understand how the colicin K N-terminal domain (KT) interacts with the components of its transit machine in the perip

SUBMITTER: Barneoud-Arnoulet A 

PROVIDER: S-EPMC2976459 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature