Next Article in Journal
Respiratory Effects of Sarafotoxins from the Venom of Different Atractaspis Genus Snake Species
Next Article in Special Issue
Mapping Protein–Protein Interactions of the Resistance-Related Bacterial Zeta Toxin–Epsilon Antitoxin Complex (ε2ζ2) with High Affinity Peptide Ligands Using Fluorescence Polarization
Previous Article in Journal
Baltikinin: A New Myotropic Tryptophyllin-3 Peptide Isolated from the Skin Secretion of the Purple-Sided Leaf Frog, Phyllomedusa baltea
Previous Article in Special Issue
Characterization of the Deep-Sea Streptomyces sp. SCSIO 02999 Derived VapC/VapB Toxin-Antitoxin System in Escherichia coli
Open AccessReview

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

Department of Chemistry and Biochemistry, University of Oklahoma, Norman, OK 73019, USA
*
Author to whom correspondence should be addressed.
Academic Editor: Anton Meinhart
Toxins 2016, 8(7), 214; https://doi.org/10.3390/toxins8070214
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)
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
Show Figures

Graphical abstract

MDPI and ACS Style

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

AMA Style

Muthuramalingam M, White JC, Bourne CR. Toxin-Antitoxin Modules Are Pliable Switches Activated by Multiple Protease Pathways. Toxins. 2016; 8(7):214.

Chicago/Turabian Style

Muthuramalingam, Meenakumari; White, John C.; Bourne, Christina R. 2016. "Toxin-Antitoxin Modules Are Pliable Switches Activated by Multiple Protease Pathways" Toxins 8, no. 7: 214.

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Search more from Scilit
 
Search
Back to TopTop