ArticleThe Journal of biological chemistry2009
Driving forces of gyrase recognition by the addiction toxin CcdB.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 27 citations in OpenAlex.
- Friend or Foe: Protein Inhibitors of DNA Gyrase.Biology · 2024Review
- Review
- Crystal Structure of VapBC-1 from Nontypeable Haemophilus influenzae and the Effect of PIN Domain Mutations on Survival during Infection.Journal of bacteriology · 2019Article
- Molecular mechanism governing ratio-dependent transcription regulation in the ccdAB operon.Nucleic acids research · 2017Article
- Structure, Biology, and Therapeutic Application of Toxin-Antitoxin Systems in Pathogenic Bacteria.Toxins · 2016Review
- Article
- To be or not to be: regulation of restriction-modification systems and other toxin-antitoxin systems.Nucleic acids research · 2014Review
- Recognition of human tumor necrosis factor α (TNF-α) by therapeutic antibody fragment: energetics and structural features.The Journal of biological chemistry · 2012Article
- Vibrio cholerae ParE2 poisons DNA gyrase via a mechanism distinct from other gyrase inhibitors.The Journal of biological chemistry · 2010Article
- In front of and behind the replication fork: bacterial type IIA topoisomerases.Cellular and molecular life sciences : CMLS · 2010Review
- Structural and thermodynamic characterization of Vibrio fischeri CcdB.The Journal of biological chemistry · 2010Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gyrase, an essential bacterial topoisomerase, is the target of several antibiotics (e.g. quinolones) as well as of bacterial toxin CcdB. This toxin, encoded by Escherichia coli toxin-antitoxin module ccd, poisons gyrase by causing inhibition of both transcription and replication. Because the molecular driving forces of gyrase unfolding and CcdB-gyrase binding were unknown, the nature of the CcdB-gyrase recognition remained elusive. Therefore, we performed a detailed thermodynamic analysis of CcdB binding to several fragments of gyrase A subunit (GyrA) that contain the CcdB-binding site. Binding of CcdB to the shorter fragments was studied directly by isothermal titration calorimetry. Its binding to the longer GyrA59 fragment in solution is kinetically limited and was therefore investigated via urea induced unfolding of the GyrA59-CcdB complex and unbound GyrA59 and CcdB, monitored by circular dichroism spectroscopy. Model analysis of experimental data, in combination with the relevant structural information, indicates that CcdB binding to gyrase is an enthalpic process driven mainly by specific interactions between CcdB and the highly stable dimerization domain of the GyrA. The dissection of binding energetics indicates that CcdB-gyrase recognition is accompanied by opening of the tower and catalytic domain of GyrA. Such extensive structural rearrangements appear to be crucial driving forces for the functioning of the ccd toxin-antitoxin module.
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