Next Article in Journal
Virulence Factor Genes and Antimicrobial Susceptibility of Staphylococcus aureus Strains Isolated from Blood and Chronic Wounds
Previous Article in Journal
Huntingtin and Its Role in Mechanisms of RNA-Mediated Toxicity
Previous Article in Special Issue
Different Biological Activities of Histidine-Rich Peptides Are Favored by Variations in Their Design
Correction published on 9 December 2021, see Toxins 2021, 13(12), 878.
Review

Bacterial Type I Toxins: Folding and Membrane Interactions

1
CiTCoM, CNRS, UMR 8038, Université de Paris, 93526 Paris, France
2
BRM (Bacterial Regulatory RNAs and Medicine), Inserm, UMR_S 1230, Université de Rennes 1, 35000 Rennes, France
*
Author to whom correspondence should be addressed.
These authors contributed equally.
Deceased author.
Received: 7 June 2021 / Revised: 8 July 2021 / Accepted: 9 July 2021 / Published: 14 July 2021 / Corrected: 9 December 2021
(This article belongs to the Special Issue Bacterial Toxins: Protein Folding and Membrane Interactions)
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. View Full-Text
Keywords: toxin-antitoxin systems; type I toxins; mechanisms of action; membrane depolarization; membrane permeabilization; pore formation; nucleoid condensation; structure; folding toxin-antitoxin systems; type I toxins; mechanisms of action; membrane depolarization; membrane permeabilization; pore formation; nucleoid condensation; structure; folding
Show Figures

Graphical abstract

MDPI and ACS Style

Nonin-Lecomte, S.; Fermon, L.; Felden, B.; Pinel-Marie, M.-L. Bacterial Type I Toxins: Folding and Membrane Interactions. Toxins 2021, 13, 490. https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13070490

AMA Style

Nonin-Lecomte S, Fermon L, Felden B, Pinel-Marie M-L. Bacterial Type I Toxins: Folding and Membrane Interactions. Toxins. 2021; 13(7):490. https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13070490

Chicago/Turabian Style

Nonin-Lecomte, Sylvie, Laurence Fermon, Brice Felden, and Marie-Laure Pinel-Marie. 2021. "Bacterial Type I Toxins: Folding and Membrane Interactions" Toxins 13, no. 7: 490. https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13070490

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop