4ely Citations

Alternative interactions define gyrase specificity in the CcdB family.

Abstract

Toxin-antitoxin (TA) modules are small operons associated with stress response of bacteria. F-plasmid CcdB(F) 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 CcdB(Vfi) 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.

Reviews - 4ely mentioned but not cited (1)

  1. Wake me when it's over - Bacterial toxin-antitoxin proteins and induced dormancy. Coussens NP, Daines DA. Exp Biol Med (Maywood) 241 1332-1342 (2016)


Reviews citing this publication (3)

Articles citing this publication (3)

  1. Characterization of the phd-doc and ccd toxin-antitoxin cassettes from Vibrio superintegrons. Guérout AM, Iqbal N, Mine N, Ducos-Galand M, Van Melderen L, Mazel D. J Bacteriol 195 2270-2283 (2013)
  2. Structural and biophysical characterization of Staphylococcus aureus SaMazF shows conservation of functional dynamics. Zorzini V, Buts L, Sleutel M, Garcia-Pino A, Talavera A, Haesaerts S, De Greve H, Cheung A, van Nuland NA, Loris R. Nucleic Acids Res 42 6709-6725 (2014)
  3. Expression of different ParE toxins results in conserved phenotypes with distinguishable classes of toxicity. Ames JR, Muthuramalingam M, Murphy T, Najar FZ, Bourne CR. Microbiologyopen 8 e902 (2019)