Log in

Relevant bibliographies by topics / Bacterial Toxin-antitoxin / Journal articles

To see the other types of publications on this topic, follow the link: Bacterial Toxin-antitoxin.

Journal articles on the topic 'Bacterial Toxin-antitoxin'

Author: Grafiati

Published: 6 September 2023

Last updated: 31 July 2025

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'Bacterial Toxin-antitoxin.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

Kim, Yoonji, and Jihwan Hwang. "Bacterial Toxin-antitoxin Systems and Their Biotechnological Applications." Journal of Life Science 26, no. 2 (2016): 265–74. http://dx.doi.org/10.5352/jls.2016.26.2.265.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Walling, Lauren R., and J. Scott Butler. "Structural Determinants for Antitoxin Identity and Insulation of Cross Talk between Homologous Toxin-Antitoxin Systems." Journal of Bacteriology 198, no. 24 (2016): 3287–95. http://dx.doi.org/10.1128/jb.00529-16.

Full text

Abstract:

ABSTRACT Toxin-antitoxin (TA) systems are ubiquitous in bacteria and archaea, where they play a pivotal role in the establishment and maintenance of dormancy. Under normal growth conditions, the antitoxin neutralizes the toxin. However, under conditions of stress, such as nutrient starvation or antibiotic treatment, cellular proteases degrade the antitoxin, and the toxin functions to arrest bacterial growth. We characterized the specificity determinants of the interactions between VapB antitoxins and VapC toxins from nontypeable Haemophilus influenzae (NTHi) in an effort to gain a better under

APA, Harvard, Vancouver, ISO, and other styles

3

Guglielmini, Julien, and Laurence Van Melderen. "Bacterial toxin-antitoxin systems." Mobile Genetic Elements 1, no. 4 (2011): 283–306. http://dx.doi.org/10.4161/mge.18477.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Hassan, Fatima J., Mohammed F. Al-Marjani, and Intesar N. Khelkal. "Influence of diverse pH and temperatures on the gene expression of toxin-antitoxin systems in Klebsiella pneumoniae." Advancements in Life Sciences 11, no. 4 (2024): 815. http://dx.doi.org/10.62940/als.v11i4.2836.

Full text

Abstract:

Background: The type II toxin-antitoxin system consists of tightly linked genetic units that produce a toxin and its specific antitoxin. Under typical circumstances, the antitoxin neutralizes the toxic effects caused by the toxin. However, the toxin-antitoxin systems during stress regulate bacterial growth and persistence by affecting translation or DNA replication. This study aimed to assess how variations in temperature and pH stress influence the regulation of type II toxin-antitoxin gene expression within Klebsiella pneumoniae isolates.Methods: Sixty-five Klebsiella pneumoniae isolates wer

APA, Harvard, Vancouver, ISO, and other styles

5

Bourne, Christina, Kevin Snead, and Felipe Avelino da Costa Ferreira. "Fuzzy interactions maintain cognate pairings in TA systems." Structural Dynamics 12, no. 2_Supplement (2025): A153. https://doi.org/10.1063/4.0000462.

Full text

Abstract:

Type II toxin-antitoxin (TA) ParDE systems are widespread in bacteria. The non-secreted protein toxin, ParE, potently inhibits DNA gyrase unless it is neutralized via direct interaction with the ParD antitoxin protein. ParDE operons encode cognate pairs, insulating from cross-interactions between structurally homologous ParE toxins that can reside in the same bacterial cell. These nano- to picomolar interactions are extensive and a model for "fuzzy" interactions, wherein the ParD antitoxin contains an unstructured region that is induced to fold by interactions with the ParE toxin. A major open

APA, Harvard, Vancouver, ISO, and other styles

6

Piscotta, Frank J., Philip D. Jeffrey, and A. James Link. "ParST is a widespread toxin–antitoxin module that targets nucleotide metabolism." Proceedings of the National Academy of Sciences 116, no. 3 (2018): 826–34. http://dx.doi.org/10.1073/pnas.1814633116.

Full text

Abstract:

Toxin–antitoxin (TA) systems interfere with essential cellular processes and are implicated in bacterial lifestyle adaptations such as persistence and the biofilm formation. Here, we present structural, biochemical, and functional data on an uncharacterized TA system, the COG5654–COG5642 pair. Bioinformatic analysis showed that this TA pair is found in 2,942 of the 16,286 distinct bacterial species in the RefSeq database. We solved a structure of the toxin bound to a fragment of the antitoxin to 1.50 Å. This structure suggested that the toxin is a mono-ADP-ribosyltransferase (mART). The toxin

APA, Harvard, Vancouver, ISO, and other styles

7

Singh, Charandeep, Soni Kaundal, Amar Deep, Rishita Rohilla, Maheshwaran Velusamy, and Krishan Gopal Thakur. "Structural insights into Polymorphic toxin–Immunity pair system of Bacillus subtilis." Structural Dynamics 12, no. 2_Supplement (2025): A174. https://doi.org/10.1063/4.0000483.

Full text

Abstract:

Polymorphic toxins are weapons of bacterial warfare which are being used to restrict competitors, aid kin selection and shape bacterial communities. Polymorphic toxin systems (PTS) are well studied in gram negative bacteria however there are limited studies from gram positive bacteria. In Bacillus subtilis, several members of toxin-immunity protein pairs including YeeF-YezG, YobL-Y, obK YxiD-YxxD, have been reported. There are few studies describing structural/mechanistic details of these toxin-immunity pairs. This toxin requires typeVII secretion system. We have shown that the C-terminal doma

APA, Harvard, Vancouver, ISO, and other styles

8

Nonin-Lecomte, Sylvie, Laurence Fermon, Brice Felden, and Marie-Laure Pinel-Marie. "Bacterial Type I Toxins: Folding and Membrane Interactions." Toxins 13, no. 7 (2021): 490. http://dx.doi.org/10.3390/toxins13070490.

Full text

Abstract:

Bacterial type I toxin-antitoxin systems are two-component genetic modules that encode a stable toxic protein whose ectopic overexpression can lead to growth arrest or cell death, and an unstable RNA antitoxin that inhibits toxin translation during growth. These systems are widely spread among bacterial species. Type I antitoxins are cis- or trans-encoded antisense small RNAs that interact with toxin-encoding mRNAs by pairing, thereby inhibiting toxin mRNA translation and/or inducing its degradation. Under environmental stress conditions, the up-regulation of the toxin and/or the antitoxin deg

APA, Harvard, Vancouver, ISO, and other styles

9

Manikandan, Parthasarathy, Sankaran Sandhya, Kavyashree Nadig, et al. "Identification, functional characterization, assembly and structure of ToxIN type III toxin–antitoxin complex from E. coli." Nucleic Acids Research 50, no. 3 (2022): 1687–700. http://dx.doi.org/10.1093/nar/gkab1264.

Full text

Abstract:

Abstract Toxin–antitoxin (TA) systems are proposed to play crucial roles in bacterial growth under stress conditions such as phage infection. The type III TA systems consist of a protein toxin whose activity is inhibited by a noncoding RNA antitoxin. The toxin is an endoribonuclease, while the antitoxin consists of multiple repeats of RNA. The toxin assembles with the individual antitoxin repeats into a cyclic complex in which the antitoxin forms a pseudoknot structure. While structure and functions of some type III TA systems are characterized, the complex assembly process is not well underst

APA, Harvard, Vancouver, ISO, and other styles

10

Alonso, Juan C. "Toxin–Antitoxin Systems in Pathogenic Bacteria." Toxins 13, no. 2 (2021): 74. http://dx.doi.org/10.3390/toxins13020074.

Full text

Abstract:

Toxin–antitoxin (TA) systems, which are ubiquitously present in plasmids, bacterial and archaeal genomes, are classified as types I to VI, according to the nature of the antitoxin and to the mode of toxin inhibition [...]

APA, Harvard, Vancouver, ISO, and other styles

11

Syed, Mohammad Adnan, and Céline M. Lévesque. "Chromosomal bacterial type II toxin–antitoxin systems." Canadian Journal of Microbiology 58, no. 5 (2012): 553–62. http://dx.doi.org/10.1139/w2012-025.

Full text

Abstract:

Most prokaryotic chromosomes contain a number of toxin–antitoxin (TA) modules consisting of a pair of genes that encode 2 components, a stable toxin and its cognate labile antitoxin. TA systems are also known as addiction modules, since the cells become “addicted” to the short-lived antitoxin product (the unstable antitoxin is degraded faster than the more stable toxin) because its de novo synthesis is essential for their survival. While toxins are always proteins, antitoxins are either RNAs (type I, type III) or proteins (type II). Type II TA systems are widely distributed throughout the chro

APA, Harvard, Vancouver, ISO, and other styles

12

Brantl, Sabine, and Peter Müller. "Toxin–Antitoxin Systems in Bacillus subtilis." Toxins 11, no. 5 (2019): 262. http://dx.doi.org/10.3390/toxins11050262.

Full text

Abstract:

Toxin–antitoxin (TA) systems were originally discovered as plasmid maintenance systems in a multitude of free-living bacteria, but were afterwards found to also be widespread in bacterial chromosomes. TA loci comprise two genes, one coding for a stable toxin whose overexpression kills the cell or causes growth stasis, and the other coding for an unstable antitoxin that counteracts toxin action. Of the currently known six types of TA systems, in Bacillus subtilis, so far only type I and type II TA systems were found, all encoded on the chromosome. Here, we review our present knowledge of these

APA, Harvard, Vancouver, ISO, and other styles

13

Boss, Lidia, Marcin Górniak, Alicja Lewańczyk, Joanna Morcinek-Orłowska, Sylwia Barańska, and Agnieszka Szalewska-Pałasz. "Identification of Three Type II Toxin-Antitoxin Systems in Model Bacterial Plant Pathogen Dickeya dadantii 3937." International Journal of Molecular Sciences 22, no. 11 (2021): 5932. http://dx.doi.org/10.3390/ijms22115932.

Full text

Abstract:

Type II toxin-antitoxin (TA) systems are genetic elements usually encoding two proteins: a stable toxin and an antitoxin, which binds the toxin and neutralizes its toxic effect. The disturbance in the intracellular toxin and antitoxin ratio typically leads to inhibition of bacterial growth or bacterial cell death. Despite the fact that TA modules are widespread in bacteria and archaea, the biological role of these systems is ambiguous. Nevertheless, a number of studies suggests that the TA modules are engaged in such important processes as biofilm formation, stress response or virulence and ma

APA, Harvard, Vancouver, ISO, and other styles

14

Kristoffersen, P., G. B. Jensen, K. Gerdes, and J. Piškur. "Bacterial Toxin-Antitoxin Gene System as Containment Control in Yeast Cells." Applied and Environmental Microbiology 66, no. 12 (2000): 5524–26. http://dx.doi.org/10.1128/aem.66.12.5524-5526.2000.

Full text

Abstract:

ABSTRACT The potential of a bacterial toxin-antitoxin gene system for use in containment control in eukaryotes was explored. The Escherichia coli relE and relB genes were expressed in the yeastSaccharomyces cerevisiae. Expression of therelE gene was highly toxic to yeast cells. However, expression of the relB gene counteracted the effect ofrelE to some extent, suggesting that toxin-antitoxin interaction also occurs in S. cerevisiae. Thus, bacterial toxin-antitoxin gene systems also have potential applications in the control of cell proliferation in eukaryotic cells, especially in those industr

APA, Harvard, Vancouver, ISO, and other styles

15

Damiano, Deborah K., Bruna O. P. Azevedo, George S. C. Fernandes, et al. "The Toxin of VapBC-1 Toxin-Antitoxin Module from Leptospira interrogans Is a Ribonuclease That Does Not Arrest Bacterial Growth but Affects Cell Viability." Microorganisms 12, no. 8 (2024): 1660. http://dx.doi.org/10.3390/microorganisms12081660.

Full text

Abstract:

Bacterial ubiquitous Toxin-Antitoxin (TA) systems are considered to be important survival mechanisms during stress conditions. In regular environmental conditions, the antitoxin blocks the toxin, whereas during imbalanced conditions, the antitoxin concentration decreases, exposing the bacteria cell to a range of toxic events. The most evident consequence of this disequilibrium is cell growth arrest, which is the reason why TAs are generally described as active in the function of bacterial growth kinetics. Virulence-associated proteins B and C (VapBC) are a family of type II TA system, in which

APA, Harvard, Vancouver, ISO, and other styles

16

Nieto, Concha, Izhack Cherny, Seok Kooi Khoo, et al. "The yefM-yoeB Toxin-Antitoxin Systems of Escherichia coli and Streptococcus pneumoniae: Functional and Structural Correlation." Journal of Bacteriology 189, no. 4 (2006): 1266–78. http://dx.doi.org/10.1128/jb.01130-06.

Full text

Abstract:

ABSTRACT Toxin-antitoxin loci belonging to the yefM-yoeB family are located in the chromosome or in some plasmids of several bacteria. We cloned the yefM-yoeB locus of Streptococcus pneumoniae, and these genes encode bona fide antitoxin (YefM Spn ) and toxin (YoeB Spn ) products. We showed that overproduction of YoeB Spn is toxic to Escherichia coli cells, leading to severe inhibition of cell growth and to a reduction in cell viability; this toxicity was more pronounced in an E. coli B strain than in two E. coli K-12 strains. The YoeB Spn -mediated toxicity could be reversed by the cognate ant

APA, Harvard, Vancouver, ISO, and other styles

17

Brantl, Sabine. "Bacterial type I toxin-antitoxin systems." RNA Biology 9, no. 12 (2012): 1488–90. http://dx.doi.org/10.4161/rna.23045.

Full text

APA, Harvard, Vancouver, ISO, and other styles

18

Díaz-Orejas, Ramón, Elizabeth Diago-Navarro, Ana María Hernández Arriaga, et al. "Bacterial toxin-antitoxin systems targeting translation." Journal of Applied Biomedicine 8, no. 4 (2010): 179–88. http://dx.doi.org/10.2478/v10136-009-0021-9.

Full text

APA, Harvard, Vancouver, ISO, and other styles

19

Gerdes, Kenn, and Etienne Maisonneuve. "Bacterial Persistence and Toxin-Antitoxin Loci." Annual Review of Microbiology 66, no. 1 (2012): 103–23. http://dx.doi.org/10.1146/annurev-micro-092611-150159.

Full text

APA, Harvard, Vancouver, ISO, and other styles

20

Cook, Gregory M., Jennifer R. Robson, Rebekah A. Frampton, et al. "Ribonucleases in bacterial toxin–antitoxin systems." Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms 1829, no. 6-7 (2013): 523–31. http://dx.doi.org/10.1016/j.bbagrm.2013.02.007.

Full text

APA, Harvard, Vancouver, ISO, and other styles

21

Sat, Boaz, Ronen Hazan, Tova Fisher, Hanita Khaner, Gad Glaser, and Hanna Engelberg-Kulka. "Programmed Cell Death in Escherichia coli: Some Antibiotics Can Trigger mazEFLethality." Journal of Bacteriology 183, no. 6 (2001): 2041–45. http://dx.doi.org/10.1128/jb.183.6.2041-2045.2001.

Full text

Abstract:

ABSTRACT The discovery of toxin-antitoxin gene pairs (also called addiction modules) on extrachromosomal elements of Escherichia coli, and particularly the discovery of homologous modules on the bacterial chromosome, suggest that a potential for programmed cell death may be inherent in bacterial cultures. We have reported on the E. coli mazEF system, a regulatable addiction module located on the bacterial chromosome. MazF is a stable toxin and MazE is a labile antitoxin. Here we show that cell death mediated by the E. coli mazEF module can be triggered by several antibiotics (rifampicin, chlor

APA, Harvard, Vancouver, ISO, and other styles

22

Burbank, Lindsey P., and Drake C. Stenger. "The DinJ/RelE Toxin-Antitoxin System Suppresses Bacterial Proliferation and Virulence of Xylella fastidiosa in Grapevine." Phytopathology® 107, no. 4 (2017): 388–94. http://dx.doi.org/10.1094/phyto-10-16-0374-r.

Full text

Abstract:

Xylella fastidiosa, the causal agent of Pierce’s disease of grapes, is a slow-growing, xylem-limited, bacterial pathogen. Disease progression is characterized by systemic spread of the bacterium through xylem vessel networks, causing leaf-scorching symptoms, senescence, and vine decline. It appears to be advantageous to this pathogen to avoid excessive blockage of xylem vessels, because living bacterial cells are generally found in plant tissue with low bacterial cell density and minimal scorching symptoms. The DinJ/RelE toxin-antitoxin system is characterized here for a role in controlling ba

APA, Harvard, Vancouver, ISO, and other styles

23

Fasani, Rick A., and Michael A. Savageau. "Unrelated toxin–antitoxin systems cooperate to induce persistence." Journal of The Royal Society Interface 12, no. 108 (2015): 20150130. http://dx.doi.org/10.1098/rsif.2015.0130.

Full text

Abstract:

Persisters are drug-tolerant bacteria that account for the majority of bacterial infections. They are not mutants, rather, they are slow-growing cells in an otherwise normally growing population. It is known that the frequency of persisters in a population is correlated with the number of toxin–antitoxin systems in the organism. Our previous work provided a mechanistic link between the two by showing how multiple toxin–antitoxin systems, which are present in nearly all bacteria, can cooperate to induce bistable toxin concentrations that result in a heterogeneous population of slow- and fast-gr

APA, Harvard, Vancouver, ISO, and other styles

24

Rathore, Jitendra Singh, and Lalit Kumar Gautam. "Expression, Purification, and Functional Analysis of Novel RelE Operon fromX. nematophila." Scientific World Journal 2014 (2014): 1–7. http://dx.doi.org/10.1155/2014/428159.

Full text

Abstract:

Bacterial toxin-antitoxin (TA) complexes induce programmed cell death and also function to relieve cell from stress by various response mechanisms.Escherichia coliRelB-RelE TA complex consists of a RelE toxin functionally counteracted by RelB antitoxin. In the present study, a novel homolog of RelE toxin designated as Xn-relE toxin fromXenorhabdus nematophilapossessing its own antitoxin designated as Xn-relEAT has been identified. Expression and purification of recombinant proteins under native conditions with GST and Ni-NTA chromatography prove the existence of novel TA module. The expression

APA, Harvard, Vancouver, ISO, and other styles

25

Wilbaux, Myriam, Natacha Mine, Anne-Marie Guérout, Didier Mazel, and Laurence Van Melderen. "Functional Interactions between Coexisting Toxin-Antitoxin Systems of the ccd Family in Escherichia coli O157:H7." Journal of Bacteriology 189, no. 7 (2007): 2712–19. http://dx.doi.org/10.1128/jb.01679-06.

Full text

Abstract:

ABSTRACT Toxin-antitoxin (TA) systems are widely represented on mobile genetic elements as well as in bacterial chromosomes. TA systems encode a toxin and an antitoxin neutralizing it. We have characterized a homolog of the ccd TA system of the F plasmid (ccd F) located in the chromosomal backbone of the pathogenic O157:H7 Escherichia coli strain (ccd O157). The ccd F and the ccd O157 systems coexist in O157:H7 isolates, as these pathogenic strains contain an F-related virulence plasmid carrying the ccd F system. We have shown that the chromosomal ccd O157 system encodes functional toxin and a

APA, Harvard, Vancouver, ISO, and other styles

26

El Mortaji, Lamya, Alejandro Tejada-Arranz, Aline Rifflet, et al. "A peptide of a type I toxin−antitoxin system inducesHelicobacter pylorimorphological transformation from spiral shape to coccoids." Proceedings of the National Academy of Sciences 117, no. 49 (2020): 31398–409. http://dx.doi.org/10.1073/pnas.2016195117.

Full text

Abstract:

Toxin−antitoxin systems are found in many bacterial chromosomes and plasmids with roles ranging from plasmid stabilization to biofilm formation and persistence. In these systems, the expression/activity of the toxin is counteracted by an antitoxin, which, in type I systems, is an antisense RNA. While the regulatory mechanisms of these systems are mostly well defined, the toxins’ biological activity and expression conditions are less understood. Here, these questions were investigated for a type I toxin−antitoxin system (AapA1−IsoA1) expressed from the chromosome of the human pathogenHelicobact

APA, Harvard, Vancouver, ISO, and other styles

27

Azevedo, Bruna Oliveira Pigatto, Deborah Kohn Damiano, Aline Florencio Teixeira, Ana Lucia Tabet Oller Nascimento, Luis Guilherme Virgilio Fernandes, and Alexandre Paulo Yague Lopes. "The VapBC-4 Characterization Indicates It Is a Bona Fide Toxin-Antitoxin Module of Leptospira interrogans: Initial Evidence for a Role in Bacterial Adaptation." Microorganisms 13, no. 4 (2025): 879. https://doi.org/10.3390/microorganisms13040879.

Full text

Abstract:

Toxin-antitoxin (TA) systems are one of the bacterial adaptation mechanisms to adverse conditions. Leptospira interrogans serovar Copenhageni contains nine putative TA systems. To date, only VapBC-3 and VapBC-1 have been experimentally characterized and considered functional modules. This study shows that the VapBC-4 module is a novel bona fide TA system constituted by VapB-4 antitoxin and VapC-4 toxin. Overexpression of the recombinant toxin in Escherichia coli resulted in growth inhibition, which was rescued by co-expression of the VapB-4 antitoxin. The toxin-antitoxin binding capability, es

APA, Harvard, Vancouver, ISO, and other styles

28

Kamruzzaman, Muhammad. "Editorial for Special Issue “Bacterial Toxin-Antitoxin Systems”." Microorganisms 12, no. 1 (2024): 128. http://dx.doi.org/10.3390/microorganisms12010128.

Full text

APA, Harvard, Vancouver, ISO, and other styles

29

Tamman, Hedvig, Andres Ainelo, Mari Tagel, and Rita Hõrak. "Stability of the GraA Antitoxin Depends on Growth Phase, ATP Level, and Global Regulator MexT." Journal of Bacteriology 198, no. 5 (2015): 787–96. http://dx.doi.org/10.1128/jb.00684-15.

Full text

Abstract:

ABSTRACTBacterial type II toxin-antitoxin systems consist of a potentially poisonous toxin and an antitoxin that inactivates the toxic protein by binding to it. Most of the toxins regulate stress survival, but their activation depends on the stability of the antitoxin that has to be degraded in order for the toxin to be able to attack its cellular targets. The degradation of antitoxins is usually rapid and carried out by ATP-dependent protease Lon or Clp, which is activated under stress conditions. ThegraTAsystem ofPseudomonas putidaencodes the toxin GraT, which can affect the growth rate and

APA, Harvard, Vancouver, ISO, and other styles

30

Brown, Jason M., and Karen Joy Shaw. "A Novel Family of Escherichia coli Toxin-Antitoxin Gene Pairs." Journal of Bacteriology 185, no. 22 (2003): 6600–6608. http://dx.doi.org/10.1128/jb.185.22.6600-6608.2003.

Full text

Abstract:

ABSTRACT Bacterial toxin-antitoxin protein pairs (TA pairs) encode a toxin protein, which poisons cells by binding and inhibiting an essential enzyme, and an antitoxin protein, which binds the toxin and restores viability. We took an approach that did not rely on sequence homology to search for unidentified TA pairs in the genome of Escherichia coli K-12. Of 32 candidate genes tested, ectopic expression of 6 caused growth inhibition. In this report, we focus on the initial characterization of yeeV, ykfI, and ypjF, a novel family of toxin proteins. Coexpression of the gene upstream of each toxi

APA, Harvard, Vancouver, ISO, and other styles

31

Zamakhaev, M. V., A. V. Goncharenko, and M. S. Shumkov. "Toxin-Antitoxin Systems and Bacterial Persistence (Review)." Applied Biochemistry and Microbiology 55, no. 6 (2019): 571–81. http://dx.doi.org/10.1134/s0003683819060140.

Full text

APA, Harvard, Vancouver, ISO, and other styles

32

Akarsu, Hatice, Patricia Bordes, Moise Mansour, Donna-Joe Bigot, Pierre Genevaux, and Laurent Falquet. "TASmania: A bacterial Toxin-Antitoxin Systems database." PLOS Computational Biology 15, no. 4 (2019): e1006946. http://dx.doi.org/10.1371/journal.pcbi.1006946.

Full text

APA, Harvard, Vancouver, ISO, and other styles

33

Zielenkiewicz, Urszula, and Piotr Cegłowski. "The Toxin-Antitoxin System of the Streptococcal Plasmid pSM19035." Journal of Bacteriology 187, no. 17 (2005): 6094–105. http://dx.doi.org/10.1128/jb.187.17.6094-6105.2005.

Full text

Abstract:

ABSTRACT pSM19035 of the pathogenic bacterium Streptococcus pyogenes is a low-copy-number plasmid carrying erythromycin resistance, stably maintained in a broad range of gram-positive bacteria. We show here that the ω-ε-ζ operon of this plasmid constitutes a novel proteic plasmid addiction system in which the ε and ζ genes encode an antitoxin and toxin, respectively, while ω plays an autoregulatory function. Expression of toxin Zeta is bactericidal for the gram-positive Bacillus subtilis and bacteriostatic for the gram-negative Escherichia coli. The toxic effects of ζ gene expression in both b

APA, Harvard, Vancouver, ISO, and other styles

34

Huerta-Uribe, Alejandro, and Andrew J. Roe. "Disarming the enemy: targeting bacterial toxins with small molecules." Emerging Topics in Life Sciences 1, no. 1 (2017): 31–39. http://dx.doi.org/10.1042/etls20160013.

Full text

Abstract:

The rapid emergence of antibiotic-resistant bacterial strains has prompted efforts to find new and more efficacious treatment strategies. Targeting virulence factors produced by pathogenic bacteria has gained particular attention in the last few years. One of the inherent advantages of this approach is that it provides less selective pressure for the development of resistance mechanisms. In addition, antivirulence drugs could potentially be the answer for diseases in which the use of conventional antibiotics is counterproductive. That is the case for bacterial toxin-mediated diseases, in which

APA, Harvard, Vancouver, ISO, and other styles

35

Muñoz-Gómez, Ana J., Marc Lemonnier, Sandra Santos-Sierra, Alfredo Berzal-Herranz, and Ramón Díaz-Orejas. "RNase/Anti-RNase Activities of the Bacterial parD Toxin-Antitoxin System." Journal of Bacteriology 187, no. 9 (2005): 3151–57. http://dx.doi.org/10.1128/jb.187.9.3151-3157.2005.

Full text

Abstract:

ABSTRACT The bacterial parD toxin-antitoxin system of plasmid R1 encodes two proteins, the Kid toxin and its cognate antitoxin, Kis. Kid cleaves RNA and inhibits protein synthesis and cell growth in Escherichia coli. Here, we show that Kid promotes RNA degradation and inhibition of protein synthesis in rabbit reticulocyte lysates. These new activities of the Kid toxin were counteracted by the Kis antitoxin and were not displayed by the KidR85W variant, which is nontoxic in E. coli. Moreover, while Kid cleaved single- and double-stranded RNA with a preference for UAA or UAC triplets, KidR85W ma

APA, Harvard, Vancouver, ISO, and other styles

36

Yoshizumi, Satoshi, Yonglong Zhang, Yoshihiro Yamaguchi, Liang Chen, Barry N. Kreiswirth, and Masayori Inouye. "Staphylococcus aureus YoeB Homologues Inhibit Translation Initiation." Journal of Bacteriology 191, no. 18 (2009): 5868–72. http://dx.doi.org/10.1128/jb.00623-09.

Full text

Abstract:

ABSTRACT YoeB is a bacterial toxin encoded by the yefM-yoeB toxin-antitoxin system found in various bacterial genomes. Here, we show that Staphylococcus aureus contains two YoeB homologues, both of which function as ribosome-dependent mRNA interferases to inhibit translation initiation in a manner identical to that of YoeB-ec from Escherichia coli.

APA, Harvard, Vancouver, ISO, and other styles

37

Li, Ming, Luyao Gong, Feiyue Cheng, et al. "Toxin-antitoxin RNA pairs safeguard CRISPR-Cas systems." Science 372, no. 6541 (2021): eabe5601. http://dx.doi.org/10.1126/science.abe5601.

Full text

Abstract:

CRISPR-Cas systems provide RNA-guided adaptive immunity in prokaryotes. We report that the multisubunit CRISPR effector Cascade transcriptionally regulates a toxin-antitoxin RNA pair, CreTA. CreT (Cascade-repressed toxin) is a bacteriostatic RNA that sequesters the rare arginine tRNAUCU (transfer RNA with anticodon UCU). CreA is a CRISPR RNA–resembling antitoxin RNA, which requires Cas6 for maturation. The partial complementarity between CreA and the creT promoter directs Cascade to repress toxin transcription. Thus, CreA becomes antitoxic only in the presence of Cascade. In CreTA-deleted cell

APA, Harvard, Vancouver, ISO, and other styles

38

Encina-Robles, Josefa, Valeria Pérez-Villalobos, and Paula Bustamante. "The HicAB System: Characteristics and Biological Roles of an Underappreciated Toxin-Antitoxin System." International Journal of Molecular Sciences 25, no. 22 (2024): 12165. http://dx.doi.org/10.3390/ijms252212165.

Full text

Abstract:

Small genetic elements known as toxin-antitoxin (TA) systems are abundant in bacterial genomes and involved in stress response, phage inhibition, mobile genetic elements maintenance and biofilm formation. Type II TA systems are the most abundant and diverse, and they are organized as bicistronic operons that code for proteins (toxin and antitoxin) able to interact through a nontoxic complex. However, HicAB is one of the type II TA systems that remains understudied. Here, we review the current knowledge of HicAB systems in different bacteria, their main characteristics and the existing evidence

APA, Harvard, Vancouver, ISO, and other styles

39

Zhang, Hao, Mei Zhao, Lulu Cai, et al. "Evidence for a Functional HipBA Toxin–Antitoxin System in Acidovorax citrulli." International Journal of Molecular Sciences 26, no. 7 (2025): 3366. https://doi.org/10.3390/ijms26073366.

Full text

Abstract:

Bacterial fruit blotch (BFB) is a highly destructive seed-borne and seed-transmitted disease caused by the Gram-negative bacterium Acidovorax citrulli that has caused substantial economic losses for the cucurbit industry in China. Despite its potential for economic damage, little is known about the bacterium’s molecular mechanisms of pathogenicity. Toxin–antitoxin (TA) systems are critical for the bacterial stress response. These systems are composed of two genes, toxin and antitoxin, that encode a stable toxin protein and a labile antitoxin protein, respectively. In this study, the genes for

APA, Harvard, Vancouver, ISO, and other styles

40

Równicki, Marcin, Robert Lasek, Joanna Trylska, and Dariusz Bartosik. "Targeting Type II Toxin–Antitoxin Systems as Antibacterial Strategies." Toxins 12, no. 9 (2020): 568. http://dx.doi.org/10.3390/toxins12090568.

Full text

Abstract:

The identification of novel targets for antimicrobial agents is crucial for combating infectious diseases caused by evolving bacterial pathogens. Components of bacterial toxin–antitoxin (TA) systems have been recognized as promising therapeutic targets. These widespread genetic modules are usually composed of two genes that encode a toxic protein targeting an essential cellular process and an antitoxin that counteracts the activity of the toxin. Uncontrolled toxin expression may elicit a bactericidal effect, so they may be considered “intracellular molecular bombs” that can lead to elimination

APA, Harvard, Vancouver, ISO, and other styles

41

Lee, Min Woo, Elizabeth E. Rogers, and Drake C. Stenger. "Xylella fastidiosa Plasmid-Encoded PemK Toxin Is an Endoribonuclease." Phytopathology® 102, no. 1 (2012): 32–40. http://dx.doi.org/10.1094/phyto-05-11-0150.

Full text

Abstract:

Stable inheritance of pXF-RIV11 in Xylella fastidiosa is conferred by the pemI/pemK toxin-antitoxin (TA) system. PemK toxin inhibits bacterial growth; PemI is the corresponding antitoxin that blocks activity of PemK by direct binding. PemK and PemI were overexpressed in Escherichia coli and activities of each were assessed. Purified PemK toxin specifically degraded single-stranded RNA but not double-stranded RNA, double-stranded DNA, or single-stranded DNA. Addition of PemI antitoxin inhibited nuclease activity of PemK toxin. Purified complexes of PemI bound to PemK exhibited minimal nuclease

APA, Harvard, Vancouver, ISO, and other styles

42

Van Melderen, Laurence, and Manuel Saavedra De Bast. "Bacterial Toxin–Antitoxin Systems: More Than Selfish Entities?" PLoS Genetics 5, no. 3 (2009): e1000437. http://dx.doi.org/10.1371/journal.pgen.1000437.

Full text

APA, Harvard, Vancouver, ISO, and other styles

43

Buts, Lieven, Jurij Lah, Minh-Hoa Dao-Thi, Lode Wyns, and Remy Loris. "Toxin–antitoxin modules as bacterial metabolic stress managers." Trends in Biochemical Sciences 30, no. 12 (2005): 672–79. http://dx.doi.org/10.1016/j.tibs.2005.10.004.

Full text

APA, Harvard, Vancouver, ISO, and other styles

44

Markovski, Monica, and Sue Wickner. "Preventing Bacterial Suicide: A Novel Toxin-Antitoxin Strategy." Molecular Cell 52, no. 5 (2013): 611–12. http://dx.doi.org/10.1016/j.molcel.2013.11.018.

Full text

APA, Harvard, Vancouver, ISO, and other styles

45

Beck, Izaak N., Ben Usher, Hannah G. Hampton, Peter C. Fineran, and Tim R. Blower. "Antitoxin autoregulation of M. tuberculosis toxin-antitoxin expression through negative cooperativity arising from multiple inverted repeat sequences." Biochemical Journal 477, no. 12 (2020): 2401–19. http://dx.doi.org/10.1042/bcj20200368.

Full text

Abstract:

Toxin-antitoxin systems play key roles in bacterial adaptation, including protection from antibiotic assault and infection by bacteriophages. The type IV toxin-antitoxin system AbiE encodes a DUF1814 nucleotidyltransferase-like toxin, and a two-domain antitoxin. In Streptococcus agalactiae, the antitoxin AbiEi negatively autoregulates abiE expression through positively co-operative binding to inverted repeats within the promoter. The human pathogen Mycobacterium tuberculosis encodes four DUF1814 putative toxins, two of which have antitoxins homologous to AbiEi. One such M. tuberculosis antitox

APA, Harvard, Vancouver, ISO, and other styles

46

Ichige, Asao, and Ichizo Kobayashi. "Stability of EcoRI Restriction-Modification Enzymes In Vivo Differentiates the EcoRI Restriction-Modification System from Other Postsegregational Cell Killing Systems." Journal of Bacteriology 187, no. 19 (2005): 6612–21. http://dx.doi.org/10.1128/jb.187.19.6612-6621.2005.

Full text

Abstract:

ABSTRACT Certain type II restriction modification gene systems can kill host cells when these gene systems are eliminated from the host cells. Such ability to cause postsegregational killing of host cells is the feature of bacterial addiction modules, each of which consists of toxin and antitoxin genes. With these addiction modules, the differential stability of toxin and antitoxin molecules in cells plays an essential role in the execution of postsegregational killing. We here examined in vivo stability of the EcoRI restriction enzyme (toxin) and modification enzyme (antitoxin), the gene syst

APA, Harvard, Vancouver, ISO, and other styles

47

Saavedra De Bast, Manuel, Natacha Mine, and Laurence Van Melderen. "Chromosomal Toxin-Antitoxin Systems May Act as Antiaddiction Modules." Journal of Bacteriology 190, no. 13 (2008): 4603–9. http://dx.doi.org/10.1128/jb.00357-08.

Full text

Abstract:

ABSTRACT Toxin-antitoxin (TA) systems are widespread among bacterial chromosomes and mobile genetic elements. Although in plasmids TA systems have a clear role in their vertical inheritance by selectively killing plasmid-free daughter cells (postsegregational killing or addiction phenomenon), the physiological role of chromosomally encoded ones remains under debate. The assumption that chromosomally encoded TA systems are part of stress response networks and/or programmed cell death machinery has been called into question recently by the observation that none of the five canonical chromosomall

APA, Harvard, Vancouver, ISO, and other styles

48

Tu, Chih-Han, Michelle Holt, Shengfeng Ruan, and Christina Bourne. "Evaluating the Potential for Cross-Interactions of Antitoxins in Type II TA Systems." Toxins 12, no. 6 (2020): 422. http://dx.doi.org/10.3390/toxins12060422.

Full text

Abstract:

The diversity of Type-II toxin–antitoxin (TA) systems in bacterial genomes requires tightly controlled interaction specificity to ensure protection of the cell, and potentially to limit cross-talk between toxin–antitoxin pairs of the same family of TA systems. Further, there is a redundant use of toxin folds for different cellular targets and complexation with different classes of antitoxins, increasing the apparent requirement for the insulation of interactions. The presence of Type II TA systems has remained enigmatic with respect to potential benefits imparted to the host cells. In some cas

APA, Harvard, Vancouver, ISO, and other styles

49

Rankin, Daniel J., Leighton A. Turner, Jack A. Heinemann, and Sam P. Brown. "The coevolution of toxin and antitoxin genes drives the dynamics of bacterial addiction complexes and intragenomic conflict." Proceedings of the Royal Society B: Biological Sciences 279, no. 1743 (2012): 3706–15. http://dx.doi.org/10.1098/rspb.2012.0942.

Full text

Abstract:

Bacterial genomes commonly contain ‘addiction’ gene complexes that code for both a toxin and a corresponding antitoxin. As long as both genes are expressed, cells carrying the complex can remain healthy. However, loss of the complex (including segregational loss in daughter cells) can entail death of the cell. We develop a theoretical model to explore a number of evolutionary puzzles posed by toxin–antitoxin (TA) population biology. We first extend earlier results demonstrating that TA complexes can spread on plasmids, as an adaptation to plasmid competition in spatially structured environment

APA, Harvard, Vancouver, ISO, and other styles

50

Donegan, Niles P., Earl T. Thompson, Zhibiao Fu, and Ambrose L. Cheung. "Proteolytic Regulation of Toxin-Antitoxin Systems by ClpPC in Staphylococcus aureus." Journal of Bacteriology 192, no. 5 (2009): 1416–22. http://dx.doi.org/10.1128/jb.00233-09.

Full text

Abstract:

ABSTRACT Bacterial toxin-antitoxin (TA) systems typically consist of a small, labile antitoxin that inactivates a specific longer-lived toxin. In Escherichia coli, such antitoxins are proteolytically regulated by the ATP-dependent proteases Lon and ClpP. Under normal conditions, antitoxin synthesis is sufficient to replace this loss from proteolysis, and the bacterium remains protected from the toxin. However, if TA production is interrupted, antitoxin levels decrease, and the cognate toxin is free to inhibit the specific cellular component, such as mRNA, DnaB, or gyrase. To date, antitoxin de

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!