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TitleMolecular mechanism governing ratio-dependent transcription regulation in the ccdAB operon.
Journal, issue, pagesNucleic Acids Res, Vol. 45, Issue 6, Page 2937-2950, Year 2017
Publish dateApr 7, 2017
AuthorsAlexandra Vandervelde / Igor Drobnak / San Hadži / Yann G-J Sterckx / Thomas Welte / Henri De Greve / Daniel Charlier / Rouslan Efremov / Remy Loris / Jurij Lah /
PubMed AbstractBacteria can become transiently tolerant to several classes of antibiotics. This phenomenon known as persistence is regulated by small genetic elements called toxin-antitoxin modules with intricate ...Bacteria can become transiently tolerant to several classes of antibiotics. This phenomenon known as persistence is regulated by small genetic elements called toxin-antitoxin modules with intricate yet often poorly understood self-regulatory features. Here, we describe the structures of molecular complexes and interactions that drive the transcription regulation of the ccdAB toxin-antitoxin module. Low specificity and affinity of the antitoxin CcdA2 for individual binding sites on the operator are enhanced by the toxin CcdB2, which bridges the CcdA2 dimers. This results in a unique extended repressing complex that spirals around the operator and presents equally spaced DNA binding sites. The multivalency of binding sites induces a digital on-off switch for transcription, regulated by the toxin:antitoxin ratio. The ratio at which this switch occurs is modulated by non-specific interactions with the excess chromosomal DNA. Altogether, we present the molecular mechanisms underlying the ratio-dependent transcriptional regulation of the ccdAB operon.
External linksNucleic Acids Res / PubMed:28334797 / PubMed Central
MethodsEM (helical sym.)
Resolution23.0 - 25.0 Å
Structure data

EMDB-3568:
3D reconstruction for the thin CcdA-CcdB-DNA filaments based on the negative stain electron microscopy dataset.
Method: EM (helical sym.) / Resolution: 23.0 Å

EMDB-3569:
3D reconstruction for the thick CcdA-CcdB-DNA filaments based on the cryo-electron microscopy dataset.
Method: EM (helical sym.) / Resolution: 25.0 Å

Source
  • Escherichia coli K-12 (bacteria)
  • Escherichia coli (E. coli)

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