An Escherichia coli K-12 strain and its mutant, temperature-sensitive in deoxyribonucleic acid (DNA) synthesis, were used as hosts for two different ColB factors (ColB3-K166 and ColB4-K98). Induction of either colicin occurred in both hosts in the presence of mitomycin C at 42 C. Induction of the temperature-sensitive colicinogenic hosts also occurred without mitomycin C at 42 C at which temper...

The three-dimensional solution structure of the colicin E3 immunity protein (84 residues) was determined by distance geometry calculations. The hydrophilic side of a four-stranded antiparallel beta-sheet constitutes a part of the surface of the protein, and two loops lie on the hydrophobic side of the sheet. All the three specificity-determining residues, which are included in the center of the...

The ferrichrome-iron receptor encoded by the fhuA gene of Escherichia coli K-12 is a multifunctional outer membrane receptor required for the binding and uptake of ferrichrome and bacteriophages T5, T1, phi 80, and UC-1 as well as colicin M. To identify domains of the protein which are important for FhuA activities, a library of 31 overlapping deletion mutants in the fhuA gene was generated. Ex...

The natively disordered N-terminal 83-aa translocation (T) domain of E group nuclease colicins recruits OmpF to a colicin-receptor complex in the outer membrane (OM) as well as TolB in the periplasm of Escherichia coli, the latter triggering translocation of the toxin across the OM. We have identified the 16-residue TolB binding epitope in the natively disordered T-domain of the nuclease colici...

Colicin K was purified from Escherichia coli K-235 (Col K) as a single protein free from polysaccharide. Its molecular weight was estimated at 70,000.