Characterization of the receptor and translocator domains of colicin N

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Abstract
Intact colicin N and various colicin derivatives, including a natural fragment lacking the first 36 amino-acid residues, a chymotryptic fragment lacking the first 66 amino acids and a thermolytic fragment comprising residues 183-387, were used to locate the regions involved in colicin-N uptake by sensitive Escherichia coli cells. Two separate domains of the molecule participate in colicin-N entry. Specific binding to OmpF receptor site requires a region located between residues 67-182. A N-terminal domain, located between residues 17-66, is involved during the translocation step after binding to receptor. Two sub-regions, residues 17-36 and residues 37-36, can be defined in this domain. The location and interactions between these domains are discussed in comparison to other colicins which use similar cell components for their uptake.