Please use this identifier to cite or link to this item:https://hdl.handle.net/20.500.12259/42919
Type of publication: Straipsnis Clarivate Analytics Web of Science ar/ir Scopus / Article in Clarivate Analytics Web of Science or / and Scopus (S1)
Field of Science: Biochemija / Biochemistry (N004)
Author(s): Lioy, Virginia S;Machon, Cristina;Tabone, Mariangela;Gonzalez-Pastor, José E;Daugelavičius, Rimantas;Ayora, Silvia;Alonso, Juan C
Title: The ζ toxin induces a set of protective responses and dormancy
Is part of: PLoS ONE [elektroninis išteklius]. San Francisco, USA : Public Library of Science, 2012, vol. 7, iss. 1
Extent: p. 1-12
Date: 2012
Keywords: Toxin ζ;Antitoxin protein;TA module
Abstract: The ζε module consists of a labile antitoxin protein, ε, which in dimer form (ε2) interferes with the action of the long-living monomeric ζ phosphotransferase toxin through protein complex formation. Toxin ζ, which inhibits cell wall biosynthesis and may be bactericide in nature, at or near physiological concentrations induces reversible cessation of Bacillus subtilis proliferation (protective dormancy) by targeting essential metabolic functions followed by propidium iodide (PI) staining in a fraction (20–30%) of the population and selects a subpopulation of cells that exhibit non-inheritable tolerance (1–5×10−5). Early after induction ζ toxin alters the expression of ~78 genes, with the up-regulation of relA among them. RelA contributes to enforce toxin-induced dormancy. At later times, free active ζ decreases synthesis of macromolecules and releases intracellular K+. We propose that ζ toxin induces reversible protective dormancy and permeation to PI, and expression of ε2 antitoxin reverses these effects. At later times, toxin expression is followed by death of a small fraction (~10%) of PI stained cells that exited earlier or did not enter into the dormant state. Recovery from stress leads to de novo synthesis of ε2 antitoxin, which blocks ATP binding by ζ toxin, thereby inhibiting its phosphotransferase activity
Internet: http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0030282
Affiliation(s): Biochemijos katedra
Gamtos mokslų fakultetas
Vytauto Didžiojo universitetas
Appears in Collections:Universiteto mokslo publikacijos / University Research Publications

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