Adenylylation of Gyrase and Topo IV by FicT Toxins Disrupts Bacterial DNA Topology
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 3237427
Author(s) Harms, Alexander; Stanger, Frédéric Valentin; Scheu, Patrick Daniel; de Jong, Imke Greet; Goepfert, Arnaud; Glatter, Timo; Gerdes, Kenn; Schirmer, Tilman; Dehio, Christoph
Author(s) at UniBasel Schirmer, Tilman
Dehio, Christoph
Stanger, Frédéric
Glatter, Timo
de Jong, Imke
Harms, Alexander
Year 2015
Title Adenylylation of Gyrase and Topo IV by FicT Toxins Disrupts Bacterial DNA Topology
Journal Cell Reports
Volume 12
Number 9
Pages / Article-Number 1497-507
Mesh terms Bacterial Toxins, metabolism; DNA Gyrase, metabolism; DNA Topoisomerase IV, metabolism; DNA, Bacterial, metabolism; Escherichia coli, metabolism; Escherichia coli Proteins, metabolism; Nucleic Acid Conformation; Pseudomonas aeruginosa, metabolism
Abstract Toxin-antitoxin (TA) modules are ubiquitous molecular switches controlling bacterial growth via the release of toxins that inhibit cell proliferation. Most of these toxins interfere with protein translation, but a growing variety of other mechanisms hints at a diversity that is not yet fully appreciated. Here, we characterize a group of FIC domain proteins as toxins of the conserved and abundant FicTA family of TA modules, and we reveal that they act by suspending control of cellular DNA topology. We show that FicTs are enzymes that adenylylate DNA gyrase and topoisomerase IV, the essential bacterial type IIA topoisomerases, at their ATP-binding site. This modification inactivates both targets by blocking their ATPase activity, and, consequently, causes reversible growth arrest due to the knotting, catenation, and relaxation of cellular DNA. Our results give insight into the regulation of DNA topology and highlight the remarkable plasticity of FIC domain proteins.
Publisher Cell Press
ISSN/ISBN 2211-1247
URL http://www.ncbi.nlm.nih.gov/pubmed/26299961
edoc-URL http://edoc.unibas.ch/39482/
Full Text on edoc Available
Digital Object Identifier DOI 10.1016/j.celrep.2015.07.056
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/26299961
ISI-Number WOS:000360574200013
Document type (ISI) Journal Article
 
   

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