Bifurcated binding of the OmpF receptor underpins import of the bacteriocin colicin N into Escherichia coli.

ABSTRACT: Colicins are Escherichia coli-specific bacteriocins that translocate across the outer bacterial membrane by a poorly understood mechanism. Group A colicins typically parasitize the proton-motive force-linked Tol system in the inner membrane via porins after first binding an outer membrane protein receptor. Recent studies have suggested that the pore-forming group A colicin N (ColN) instead uses lipopolysaccharide as a receptor. Contrary to this prevailing view, using diffusion-precipitation assays, native state MS, isothermal titration calorimetry, single-channel conductance measurements in planar lipid bilayers, and in vivo fluorescence imaging, we demonstrate here that ColN uses OmpF both as its receptor and translocator. This dual function is achieved by ColN having multip

SUBMITTER: Jansen KB 

PROVIDER: S-EPMC7335789 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature