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- W3186472822 endingPage "490" @default.
- W3186472822 startingPage "490" @default.
- W3186472822 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 degradation by specific RNases promote toxin translation. Most type I toxins are small hydrophobic peptides with a predicted α-helical transmembrane domain that induces membrane depolarization and/or permeabilization followed by a decrease of intracellular ATP, leading to plasmid maintenance, growth adaptation to environmental stresses, or persister cell formation. In this review, we describe the current state of the art on the folding and the membrane interactions of these membrane-associated type I toxins from either Gram-negative or Gram-positive bacteria and establish a chronology of their toxic effects on the bacterial cell. This review also includes novel structural results obtained by NMR concerning the sprG1-encoded membrane peptides that belong to the sprG1/SprF1 type I TA system expressed in Staphylococcus aureus and discusses the putative membrane interactions allowing the lysis of competing bacteria and host cells." @default.
- W3186472822 created "2021-08-02" @default.
- W3186472822 creator A5008739452 @default.
- W3186472822 creator A5026912110 @default.
- W3186472822 creator A5041880509 @default.
- W3186472822 creator A5072124592 @default.
- W3186472822 date "2021-07-14" @default.
- W3186472822 modified "2023-10-13" @default.
- W3186472822 title "Bacterial Type I Toxins: Folding and Membrane Interactions" @default.
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- W3186472822 doi "https://doi.org/10.3390/toxins13070490" @default.