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

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...

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Autores principales: Muthuramalingam, Meenakumari, White, John C., Bourne, Christina R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4963847/
https://www.ncbi.nlm.nih.gov/pubmed/27409636
http://dx.doi.org/10.3390/toxins8070214
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author Muthuramalingam, Meenakumari
White, John C.
Bourne, Christina R.
author_facet Muthuramalingam, Meenakumari
White, John C.
Bourne, Christina R.
author_sort Muthuramalingam, Meenakumari
collection PubMed
description 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.
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spelling pubmed-49638472016-08-03 Toxin-Antitoxin Modules Are Pliable Switches Activated by Multiple Protease Pathways Muthuramalingam, Meenakumari White, John C. Bourne, Christina R. Toxins (Basel) Review 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. MDPI 2016-07-09 /pmc/articles/PMC4963847/ /pubmed/27409636 http://dx.doi.org/10.3390/toxins8070214 Text en © 2016 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Muthuramalingam, Meenakumari
White, John C.
Bourne, Christina R.
Toxin-Antitoxin Modules Are Pliable Switches Activated by Multiple Protease Pathways
title Toxin-Antitoxin Modules Are Pliable Switches Activated by Multiple Protease Pathways
title_full Toxin-Antitoxin Modules Are Pliable Switches Activated by Multiple Protease Pathways
title_fullStr Toxin-Antitoxin Modules Are Pliable Switches Activated by Multiple Protease Pathways
title_full_unstemmed Toxin-Antitoxin Modules Are Pliable Switches Activated by Multiple Protease Pathways
title_short Toxin-Antitoxin Modules Are Pliable Switches Activated by Multiple Protease Pathways
title_sort toxin-antitoxin modules are pliable switches activated by multiple protease pathways
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4963847/
https://www.ncbi.nlm.nih.gov/pubmed/27409636
http://dx.doi.org/10.3390/toxins8070214
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