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  4. Toxin:antitoxin ratio sensing autoregulation of the <i>Vibrio cholerae parDE2</i> module
 
research article

Toxin:antitoxin ratio sensing autoregulation of the Vibrio cholerae parDE2 module

Garcia Rodriguez, Gabriela  
•
Girardin, Y
•
Singh, RK
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January 5, 2024
Science Advances

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.

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Type
research article
DOI
10.1126/sciadv.adj2403
Web of Science ID

WOS:001142521700007

Author(s)
Garcia Rodriguez, Gabriela  
Girardin, Y
Singh, RK
Volkov, AN
Muruganandam, G
Loris, R
Van Dyck, J
Sobott, F
Charlier, D
Date Issued

2024-01-05

Published in
Science Advances
Volume

10

Issue

1

Subjects

Toxin-Antitoxin Systems

•

Molecular-Structure Determination

•

Range Plasmid Rk2

•

Escherichia-Coli

•

Dna-Binding

•

Xplor-Nih

•

Functional-Analysis

•

Crystal-Structure

•

Structural Basis

•

Nmr Structures

Editorial or Peer reviewed

REVIEWED

Written at

OTHER

EPFL units
UPGON  
FunderGrant Number

FWO- Vlaanderen

G.0226.17N

Vrije Universiteit Brussel

SPR13

INEXT

4146

Available on Infoscience
February 2, 2024
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/203426
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