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Structure and Function of Bacterial Kid-Kis and Related Toxin-Antitoxin Systems

[ Vol. 14 , Issue. 2 ]


Monique B. Kamphuis, Maria Chiara Monti, Robert H. H. van den Heuvel, Juan Lopez-Villarejo, Ramon Diaz-Orejas and Rolf Boelens   Pages 113 - 124 ( 12 )


Toxin-antitoxin systems were discovered as plasmid auxiliary maintenance cassettes. In recent years, an increasing amount of structural and functional information has become available about the proteins involved, allowing the understanding of bacterial cell growth inhibition by the toxins on a molecular level. A well-studied TA system is formed by the proteins Kid and Kis, encoded by the parD operon of the Escherichia coli plasmid R1. The toxicity of Kid has been related to its endoribonuclease activity, which is counteracted by binding of the antitoxin Kis at the proposed active site. In this review, the structural studies on the Kid-Kis system are compared to those of three related toxin-antitoxin systems: MazF-MazE, CcdB-CcdA and RelE-RelB.


CcdB-CcdA, MazF-MazE, plasmid maintenance, RelE-RelB, ribonuclease


Department of NMR Spectroscopy,Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.

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