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...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2016-07-01
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| Series: | Toxins |
| Subjects: | |
| Online Access: | http://www.mdpi.com/2072-6651/8/7/214 |
| _version_ | 1828120197833162752 |
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| author | Meenakumari Muthuramalingam John C. White Christina R. Bourne |
| author_facet | Meenakumari Muthuramalingam John C. White Christina R. Bourne |
| author_sort | Meenakumari Muthuramalingam |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-04-11T14:01:19Z |
| format | Article |
| id | doaj.art-3a2c64c898634cc3960dc758eea1cd56 |
| institution | Directory Open Access Journal |
| issn | 2072-6651 |
| language | English |
| last_indexed | 2024-04-11T14:01:19Z |
| publishDate | 2016-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Toxins |
| spelling | doaj.art-3a2c64c898634cc3960dc758eea1cd562022-12-22T04:20:06ZengMDPI AGToxins2072-66512016-07-018721410.3390/toxins8070214toxins8070214Toxin-Antitoxin Modules Are Pliable Switches Activated by Multiple Protease PathwaysMeenakumari Muthuramalingam0John C. White1Christina R. Bourne2Department of Chemistry and Biochemistry, University of Oklahoma, Norman, OK 73019, USADepartment of Chemistry and Biochemistry, University of Oklahoma, Norman, OK 73019, USADepartment of Chemistry and Biochemistry, University of Oklahoma, Norman, OK 73019, USAToxin-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.http://www.mdpi.com/2072-6651/8/7/214toxin-antitoxinphenotypic changespersister cellspost-segregational killingbacterial physiologyenvironmental adaptationcellular proteasesprotease adaptors |
| spellingShingle | Meenakumari Muthuramalingam John C. White Christina R. Bourne Toxin-Antitoxin Modules Are Pliable Switches Activated by Multiple Protease Pathways Toxins toxin-antitoxin phenotypic changes persister cells post-segregational killing bacterial physiology environmental adaptation cellular proteases protease adaptors |
| 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 | toxin-antitoxin phenotypic changes persister cells post-segregational killing bacterial physiology environmental adaptation cellular proteases protease adaptors |
| url | http://www.mdpi.com/2072-6651/8/7/214 |
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