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Toxins 2016, 8(7), 214; doi:10.3390/toxins8070214

Toxin-Antitoxin Modules Are Pliable Switches Activated by Multiple Protease Pathways

Department of Chemistry and Biochemistry, University of Oklahoma, Norman, OK 73019, USA
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Author to whom correspondence should be addressed.
Academic Editor: Anton Meinhart
Received: 14 May 2016 / Revised: 24 June 2016 / Accepted: 27 June 2016 / Published: 9 July 2016
(This article belongs to the Special Issue Toxin-Antitoxin System in Bacteria)
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Abstract

Toxin-antitoxin (TA) modules are bacterial regulatory switches that facilitate conflicting outcomes for cells by promoting a pro-survival phenotypic adaptation and/or by directly mediating cell death, all through the toxin activity upon degradation of antitoxin. Intensive study has revealed specific details of TA module functions, but significant gaps remain about the molecular details of activation via antitoxin degradation used by different bacteria and in different environments. This review summarizes the current state of knowledge about the interaction of antitoxins with cellular proteases Lon and ClpP to mediate TA module activation. An understanding of these processes can answer long-standing questions regarding stochastic versus specific activation of TA modules and provide insight into the potential for manipulation of TA modules to alter bacterial growth. View Full-Text
Keywords: toxin-antitoxin; phenotypic changes; persister cells; post-segregational killing; bacterial physiology; environmental adaptation; cellular proteases; protease adaptors toxin-antitoxin; phenotypic changes; persister cells; post-segregational killing; bacterial physiology; environmental adaptation; cellular proteases; protease adaptors
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Muthuramalingam, M.; White, J.C.; Bourne, C.R. Toxin-Antitoxin Modules Are Pliable Switches Activated by Multiple Protease Pathways. Toxins 2016, 8, 214.

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