» Articles » PMID: 38138007

The Benefits of Toxicity: VapBC TA Module Is Induced by Tetracycline Exposure and Promotes Survival

Overview
Journal Microorganisms
Specialty Microbiology
Date 2023 Dec 23
PMID 38138007
Authors
Affiliations
Soon will be listed here.
Abstract

Toxin-antitoxin (TA) systems are widely present in bacterial genomes. , a common model organism for studying physiology, has eight TA loci, including and . This study aims to investigate the physiological significance of these TA systems. Proteomic profiling was conducted on a culture overexpressing the VapC toxin, and the involvement of VapC in stress responses to heat shock and antibiotic treatment was examined. While deciphering the underlying mechanisms of the altered stress resistance, we assessed the antibiotic susceptibility of , , and double deletion mutants. Additionally, the mRNA levels of and were measured following tetracycline supplementation. The results reveal changes in the abundance of metabolic enzymes and stress response proteins associated with VapC overexpression. This activation of the general stress response leads to reduced thermosensitivity in , but does not affect susceptibility to ciprofloxacin and isoniazid. Under tetracycline treatment, both and expression levels are increased, and the fate of the cell depends on the interaction between the corresponding TA systems.

References
1.
Sartain M, Dick D, Rithner C, Crick D, Belisle J . Lipidomic analyses of Mycobacterium tuberculosis based on accurate mass measurements and the novel "Mtb LipidDB". J Lipid Res. 2011; 52(5):861-72. PMC: 3073466. DOI: 10.1194/jlr.M010363. View

2.
Cheetham M, Caplan A . Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function. Cell Stress Chaperones. 1998; 3(1):28-36. PMC: 312945. DOI: 10.1379/1466-1268(1998)003<0028:sfaeod>2.3.co;2. View

3.
De Biase D, Pennacchietti E . Glutamate decarboxylase-dependent acid resistance in orally acquired bacteria: function, distribution and biomedical implications of the gadBC operon. Mol Microbiol. 2012; 86(4):770-86. DOI: 10.1111/mmi.12020. View

4.
Zamakhaev M, Grigorov A, Bespyatykh J, Azhikina T, Goncharenko A, Shumkov M . VapC toxin switches M. smegmatis cells into dormancy through 23S rRNA cleavage. Arch Microbiol. 2022; 205(1):28. DOI: 10.1007/s00203-022-03363-1. View

5.
Baker T, Sauer R . ClpXP, an ATP-powered unfolding and protein-degradation machine. Biochim Biophys Acta. 2011; 1823(1):15-28. PMC: 3209554. DOI: 10.1016/j.bbamcr.2011.06.007. View