Purification and characterization of a complex between cloacin and its immunity protein isolated from Enterobacter cloacae (Clo DF13). Dissociation and reconstitution of the complex.
Cell of Enterobacter cloacae (Clo DF13) produce a bacteriocin which is characterized by its very effective killing activity against sensitive bacteria. Purification and characterization of the excreted bacteriocin has revealed that this bacteriocin consists of an equimolar complex of two plasmid-specific gene products: the cloacin and its inhibitor the immunity protein. Dissociation of the complex by treatment with sodium dodecylsulfate induces the endonucleolytic activity of the cloacin but strongly reduces the killing activity. The purified complex possesses no activity in vitro. Both cloacin and immunity protein isolated from the complex were functionally identical to cloacin and immunity protein purified from the bacteriocinogenic cells by other methods. Reconstitution of the complex results in a partial restoration of killing activity.
D000596:Amino Acids / Q000032:analysis; D001426:Bacterial Proteins / Q000276:immunology / Q000302:isolation & purification; D001427:Bacterial Toxins / Q000276:immunology* / Q000302:isolation & purification; D004755:Enterobacteriaceae / Q000276:immunology*; D005779:Immunodiffusion; D007700:Kinetics; D046911:Macromolecular Substances; D011485:Protein Binding
D000596:Amino Acids; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D046911:Macromolecular Substances