Publication
Title
Alternative interactions define gyrase specificity in the CcdB family
Author
Abstract
Toxinantitoxin (TA) modules are small operons associated with stress response of bacteria. F-plasmid CcdBF was the first TA toxin for which its target, gyrase, was identified. Plasmidic and chromosomal CcdBs belong to distinct families. Conserved residues crucial for gyrase poisoning activity of plasmidic CcdBs are not conserved among these families. Here we show that the chromosomal CcdBVfi from Vibrio fischeri is an active gyrase poison that interacts with its target via an alternative energetic mechanism. Changes in the GyrA14-binding surface of the Vibrio and F-plasmid CcdB family members illustrate neutral drift where alternative interactions can be used to achieve the same functionality. Differences in affinity between V. fischeri and F-plasmid CcdB for gyrase and their corresponding CcdA antitoxin possibly reflect distinct roles for TA modules located on plasmids and chromosomes.
Language
English
Source (journal)
Molecular microbiology. - Oxford
Publication
Oxford : 2012
ISSN
0950-382X
Volume/pages
84:5(2012), p. 965-978
ISI
000304301500011
Full text (Publisher's DOI)
Full text (publisher's version - intranet only)
UAntwerpen
Publication type
Subject
External links
Web of Science
Record
Identification
Creation 04.10.2018
Last edited 04.08.2021