Publication
Title
Toxin:antitoxin ratio sensing autoregulation of the Vibrio cholerae parDE2 module
Author
Abstract
The parDE family of toxin-antitoxin (TA) operons is ubiquitous in bacterial genomes and, in Vibrio cholerae, is an essential component to maintain the presence of chromosome II. Here, we show that transcription of the V. cholerae parDE2 (VcparDE) operon is regulated in a toxin:antitoxin ratio-dependent manner using a molecular mechanism distinct from other type II TA systems. The repressor of the operon is identified as an assembly with a 6:2 stoichiometry with three interacting ParD2 dimers bridged by two ParE2 monomers. This assembly docks to a three-site operator containing 5 '- GGTA-3 ' motifs. Saturation of this TA complex with ParE2 toxin results in disruption of the interface between ParD2 dimers and the formation of a TA complex of 2:2 stoichiometry. The latter is operator binding-incompetent as it is incompatible with the required spacing of the ParD2 dimers on the operator.
Language
English
Source (journal)
Science Advances
Publication
2024
ISSN
2375-2548
DOI
10.1126/SCIADV.ADJ2403
Volume/pages
10 :1 (2024) , p. 1-14
Article Reference
eadj2403
ISI
001142521700007
Pubmed ID
38181072
Full text (Publisher's DOI)
Full text (open access)
UAntwerpen
Publication type
Subject
Affiliation
Publications with a UAntwerp address
External links
Web of Science
Record
Identifier
Creation 01.02.2024
Last edited 04.11.2024
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