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Microbiology and Molecular Biology Reviews, March 2007, p. 158-229, Vol. 71, No. 1
1092-2172/07/$08.00+0     doi:10.1128/MMBR.00036-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Colicin Biology{dagger}

Eric Cascales,1* Susan K. Buchanan,2 Denis Duché,1 Colin Kleanthous,3 Roland Lloubès,1 Kathleen Postle,4 Margaret Riley,5 Stephen Slatin,6 and Danièle Cavard1

Laboratoire d'Ingénierie des Systèmes Macromoléculaires, Institut de Biologie Structurale et Microbiologie, Centre National de la Recherche Scientifique, UPR9027, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France,1 Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892,2 Department of Biology Area 10, P.O. Box 373, University of York, York YO10 5YW, United Kingdom,3 301 Althouse Laboratory, Department of Biochemistry and Molecular Biology, Eberly College of Science, Pennsylvania State University, University Park, Pennsylvania 16802,4 Department of Biology, University of Massachusetts at Amherst, Amherst, Massachusetts 01003,5 Department of Physiology and Biophysics, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 104616

Colicins are proteins produced by and toxic for some strains of Escherichia coli. They are produced by strains of E. coli carrying a colicinogenic plasmid that bears the genetic determinants for colicin synthesis, immunity, and release. Insights gained into each fundamental aspect of their biology are presented: their synthesis, which is under SOS regulation; their release into the extracellular medium, which involves the colicin lysis protein; and their uptake mechanisms and modes of action. Colicins are organized into three domains, each one involved in a different step of the process of killing sensitive bacteria. The structures of some colicins are known at the atomic level and are discussed. Colicins exert their lethal action by first binding to specific receptors, which are outer membrane proteins used for the entry of specific nutrients. They are then translocated through the outer membrane and transit through the periplasm by either the Tol or the TonB system. The components of each system are known, and their implication in the functioning of the system is described. Colicins then reach their lethal target and act either by forming a voltage-dependent channel into the inner membrane or by using their endonuclease activity on DNA, rRNA, or tRNA. The mechanisms of inhibition by specific and cognate immunity proteins are presented. Finally, the use of colicins as laboratory or biotechnological tools and their mode of evolution are discussed.

* Corresponding author. Mailing address: Laboratoire d'Ingénierie des Systèmes Macromoléculaires, IBSM, CNRS UPR9027, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France. Phone: (33) 491 164 663. Fax: (33) 491 712 124. E-mail: cascales{at}ibsm.cnrs-mrs.fr.

{dagger} This review is dedicated to Robert Kadner (1942-2005).

Microbiology and Molecular Biology Reviews, March 2007, p. 158-229, Vol. 71, No. 1
1092-2172/07/$08.00+0     doi:10.1128/MMBR.00036-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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