Toxin:antitoxin ratio sensing autoregulation of the Vibrio cholerae parDE2 module.
Sci Adv
; 10(1): eadj2403, 2024 Jan 05.
Article
in En
| MEDLINE
| ID: mdl-38181072
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 toxinantitoxin 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 62 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 22 stoichiometry. The latter is operator binding-incompetent as it is incompatible with the required spacing of the ParD2 dimers on the operator.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Vibrio cholerae
/
Antitoxins
Language:
En
Journal:
Sci Adv
Year:
2024
Document type:
Article
Affiliation country:
Belgium
Country of publication:
United States