Bacterial Toxin-Antitoxin Gene System as Containment Control in Yeast Cells

Kristoffersen, Peter; Jensen, Gert B.; Gerdes, Kenn; Piškur, Jure

doi:10.1128/aem.66.12.5524-5526.2000

Cited by 69 publications

(66 citation statements)

References 13 publications

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“…To achieve this, compounds that could disrupt the interactions between a toxin and its cognate antitoxin could be very useful as antibacterials: an unbalanced synthesis of each independent TAS triggers cell growth arrest or, for prolonged periods of time, cell death, with a survival rate of 1 ϫ 10 Ϫ6 to 10 Ϫ7 per each TA pair (127). Thus, it is conceivable that the employment of two independent toxins would potentiate such cell death, and indeed, TAS have been used in the design of tools for the biological containment of strains designed for bioremediation and other industrial purposes (87,123,127).…”

Section: Conclusion and Perspectives: Use Of Tas As Antimicrobialsmentioning

confidence: 99%

Toxin-Antitoxin Genes of the Gram-Positive Pathogen Streptococcus pneumoniae: So Few and Yet So Many

Chan

Moreno-Córdoba

Yeo

et al. 2012

Microbiol Mol Biol Rev

127

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SUMMARYPneumococcal infections cause up to 2 million deaths annually and raise a large economic burden and thus constitute an important threat to mankind. Because of the increase in the antibiotic resistance ofStreptococcus pneumoniaeclinical isolates, there is an urgent need to find new antimicrobial approaches to triumph over pneumococcal infections. Toxin-antitoxin (TA) systems (TAS), which are present in most living bacteria but not in eukaryotes, have been proposed as an effective strategy to combat bacterial infections. Type II TAS comprise a stable toxin and a labile antitoxin that form an innocuous TA complex under normal conditions. Under stress conditions, TA synthesis will be triggered, resulting in the degradation of the labile antitoxin and the release of the toxin protein, which would poison the host cells. The three functional chromosomal TAS fromS. pneumoniaethat have been studied as well as their molecular characteristics are discussed in detail in this review. Furthermore, a meticulous bioinformatics search has been performed for 48 pneumococcal genomes that are found in public databases, and more putative TAS, homologous to well-characterized ones, have been revealed. Strikingly, several unusual putative TAS, in terms of components and genetic organizations previously not envisaged, have been discovered and are further discussed. Previously, we reported a novel finding in which a unique pneumococcal DNA signature, the BOX element, affected the regulation of the pneumococcalyefM-yoeBTAS. This BOX element has also been found in some of the other pneumococcal TAS. In this review, we also discuss possible relationships between some of the pneumococcal TAS with pathogenicity, competence, biofilm formation, persistence, and an interesting phenomenon called bistability.

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Section: Conclusion and Perspectives: Use Of Tas As Antimicrobialsmentioning

confidence: 99%

Toxin-Antitoxin Genes of the Gram-Positive Pathogen Streptococcus pneumoniae: So Few and Yet So Many

Chan

Moreno-Córdoba

Yeo

et al. 2012

Microbiol Mol Biol Rev

127

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“…The eukaryotic pair could have originated independently, and furthermore, there is little sequence conservation among RNA targeting toxins although their general structure is conserved. Interestingly, expression of bacterial RelE in yeast restricts cell growth (Kristoffersen et al 2000) and RelE expression in mammalian cell lines can induce apoptosis (Yamamoto et al 2002), suggesting that RelE targets the translating eukaryotic ribosome and cleaves its mRNA as in Bacteria and Archae.…”

Section: Introductionmentioning

confidence: 99%

The bacterial toxin RelE induces specific mRNA cleavage in the A site of the eukaryote ribosome

Andreev¹,

Hauryliuk²,

Terenin

et al. 2007

RNA

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RelE/RelB is a well-characterized toxin-anti-toxin pair involved in nutritional stress responses in Bacteria and Archae. RelE lacks any eukaryote homolog, but we demonstrate here that it efficiently and specifically cleaves mRNA in the A site of the eukaryote ribosome. The cleavage mechanism is similar to that in bacteria, showing the feasibility of A-site cleavage of mRNA for regulatory purposes also in eukaryotes. RelE cleavage in the A-site codon of a stalled eukaryote ribosome is precise and easily monitored, making ''RelE printing'' a useful complement to toeprinting to determine the exact mRNA location on the eukaryote ribosome and to probe the occupancy of its A site.

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“…Surprisingly, Kid was found to be also toxic in eukaryotic cells, since uncoupled production of Kid and Kis triggered apoptosis in human cells and regulated cell proliferation in yeast and metazoa (9). Moreover, the chpIK system of the spirochete Leptospira interrogans, a close homologue of the E. coli parD system, was reported to be active in yeast (31), while the RelE toxin encoded by the heterologous TA system relBE of E. coli was shown to inhibit cell growth in yeast (24) and to induce apoptosis in human cells (39).…”

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confidence: 99%

RNase/Anti-RNase Activities of the BacterialparDToxin-Antitoxin System

et al. 2005

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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 maintained this sequence preference but hardly cleaved double-stranded RNA. Kid was formerly shown to inhibit DNA replication of the ColE1 plasmid. Here we provide in vitro evidence that Kid cleaves the ColE1 RNA II primer, which is required for the initiation of ColE1 replication. In contrast, KidR85W did not affect the stability of RNA II, nor did it inhibit the in vitro replication of ColE1. Thus, the endoribonuclease and the cytotoxic and DNA replication-inhibitory activities of Kid seem tightly correlated. We propose that the spectrum of action of this toxin extends beyond the sole inhibition of protein synthesis to control a broad range of RNA-regulated cellular processes.

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Bacterial Toxin-Antitoxin Gene System as Containment Control in Yeast Cells

Cited by 69 publications

References 13 publications

Toxin-Antitoxin Genes of the Gram-Positive Pathogen Streptococcus pneumoniae: So Few and Yet So Many

Toxin-Antitoxin Genes of the Gram-Positive Pathogen Streptococcus pneumoniae: So Few and Yet So Many

The bacterial toxin RelE induces specific mRNA cleavage in the A site of the eukaryote ribosome

RNase/Anti-RNase Activities of the BacterialparDToxin-Antitoxin System

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