Enzymological characterization of the nuclease domain from the bacterial toxin colicin E9 from Escherichia coli.

@article{Pommer1998EnzymologicalCO,
  title={Enzymological characterization of the nuclease domain from the bacterial toxin colicin E9 from Escherichia coli.},
  author={Ansgar J. Pommer and Russell Wallis and Geoffrey R. Moore and Richard James and Colin Kleanthous},
  journal={The Biochemical journal},
  year={1998},
  volume={334 ( Pt 2)},
  pages={387-92}
}
The cytotoxicity of the bacterial toxin colicin E9 is due to a non-specific DNase that penetrates the cytoplasm of the infected organism and causes cell death. We report the first enzymological characterization of the overexpressed and purified 15 kDa DNase domain (E9 DNase) from this class of toxin. CD spectroscopy shows the E9 DNase to be structured in solution, and analytical ultracentrifugation data indicate that the enzyme is a monomer. The nuclease activity of the E9 DNase was compared… CONTINUE READING
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