The biology of E colicins: paradigms and paradoxes

Article Abstract:

There are biological problems in studying the mode of action, inhibition, and immunity of the nuclease-type E colicins. E colicins are antibacterial, plasmid-encoded proteins that bind to the product of the chromosomal btuB gene in Escherichia coli, forming an E9-Im9 complex. The nature of the fragment causing the cytotoxic activity and the end product of Im9 is unknown. Information about these processes may have applications in antibiotic development. The protein-protein interactions between E colicins and immunity proteins, and the evolution of E colicins are discussed.

Analysis, Antibacterial agents, Cell-mediated cytotoxicity, Cell mediated cytotoxicity

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Binding of colicins A and E1 to purified ToIA domains

Article Abstract:

A research on the binding of colicins A and E1 and their interaction with ToIA soluble derivatives was conducted. Research methodologies included plasmid constructs, purification of ToIA derivatives and N-terminal domains of colicins A and E1, Western blotting and peptide analysis. Results showed that the N-terminal domain of colicin E1 and A can interact with the C terminal of TolA. Furthermore, the binding of colicins A and E1 to ToIA were estimated by surface plasmon resonance and were shown to be similar.

Bacteria, Protein binding, Membrane fusion

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Identification of residues in the putative TolA box which are essential for the toxicity of the endonuclease toxin colicin E9

Article Abstract:

A study was conducted on five putative TolA box residues to determine their role in the endonuclease toxin colicin E9's biological activity. The residues were change into alanines using site-directed mutagenesis. Results have shown that the biological activity of the mutant colicin E9 was not affected by the mutagenesis of two serine residues flanking the putative TolA box, Ser34 and Ser40, and the TolA box is involved in the translocation of colicin E9.

Escherichia coli, Mutagenesis

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