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Linking bacterial type I toxins with their actions

Journal

CURRENT OPINION IN MICROBIOLOGY
Volume 30, Issue -, Pages 114-121

Publisher

CURRENT BIOLOGY LTD
DOI: 10.1016/j.mib.2016.01.009

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Funding

  1. University of Rennes 1 (France)
  2. University of Bern (Switzerland)
  3. University of Sherbrooke (Canada)
  4. 'Institut National de la Sante et de la Recherche Medicale' (INSERM)
  5. School of Pharmacy and Medical Sciences of Rennes 1 University
  6. French Medical Research Foundation (FRM)

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Bacterial type I toxin-antitoxin systems consist of stable toxin encoding mRNAs whose expression is counteracted by unstable RNA antitoxins. Accumulating evidence suggests that these players belong to broad regulatory networks influencing overall bacterial physiology. The majority of known transmembrane type I toxic peptides have conserved structural characteristics. However, recent studies demonstrated that their mechanisms of toxicity are diverse and complex. To better assess the current state of the art, type I toxins can be grouped into two classes according to their location and mechanisms of action: membrane-associated toxins acting by pore formation and/or by nucleoid condensation; and cytosolic toxins inducing nucleic acid cleavage. This classification will evolve as a result of future investigations.

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