Enterococcus faecalisPlasmid pAD1-Encoded Fst Toxin Affects Membrane Permeability and Alters Cellular Responses to Lantibiotics
Open Access
- 1 April 2003
- journal article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 185 (7) , 2169-2177
- https://doi.org/10.1128/jb.185.7.2169-2177.2003
Abstract
Fst is a peptide toxin encoded by thepartoxin-antitoxin stability determinant ofEnterococcus faecalisplasmid pAD1. Intracellular overproduction of Fst resulted in simultaneous inhibition of all cellular macromolecular synthesis concomitant with cell growth inhibition and compromised the integrity of the cell membrane. Cells did not lyse or noticeably leak intracellular contents but had specific defects in chromosome partitioning and cell division. Extracellular addition of synthetic Fst had no effect on cell growth. Spontaneous Fst-resistant mutants had a phenotype consistent with changes in membrane composition. Interestingly, overproduction of Fst sensitized cells to the lantibiotic nisin, and Fst-resistant mutants were cross-resistant to nisin and the pAD1-encoded cytolysin.Keywords
This publication has 48 references indexed in Scilit:
- Molecular characterization of long direct repeat (LDR) sequences expressing a stable mRNA encoding for a 35‐amino‐acid cell‐killing peptide and a cis‐encoded small antisense RNA in Escherichia coliMolecular Microbiology, 2002
- Two-component regulator of Enterococcus faecalis cytolysin responds to quorum-sensing autoinductionNature, 2002
- Lantibiotics: structure, biosynthesis and mode of actionFEMS Microbiology Reviews, 2001
- Structural analysis and proteolytic activation of Enterococcus faecalis cytolysin, a novel lantibioticMolecular Microbiology, 1996
- Programmed cell death in bacteria: translational repression by mRNA end‐pairingMolecular Microbiology, 1996
- Functional analysis of the Enterococcus faecalis plasmid pAD1‐encoded stability determinant parMolecular Microbiology, 1996
- Mechanism of Post-segregational Killing: Secondary Structure Analysis of the Entire Hok mRNA from Plasmid R1 Suggests a Fold-back Structure that Prevents Translation and Antisense RNA BindingJournal of Molecular Biology, 1995
- Kid, a small protein of the parD stability system of plasmid R1, is an inhibitor of DNA replication acting at the initiation of DNA synthesisJournal of Molecular Biology, 1995
- Cell killing by the F plasmid CcdB protein involves poisoning of DNA-topoisomerase II complexesJournal of Molecular Biology, 1992
- Mechanism of killer gene activation. Antisense RNA-dependent RNase III cleavage ensures rapid turn-over of the stable Hok, SrnB and PndA effector messenger RNAsJournal of Molecular Biology, 1992