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TitleAntibiotic thermorubin tethers ribosomal subunits and impedes A-site interactions to perturb protein synthesis in bacteria.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 918, Year 2023
Publish dateFeb 17, 2023
AuthorsNarayan Prasad Parajuli / Andrew Emmerich / Chandra Sekhar Mandava / Michael Y Pavlov / Suparna Sanyal /
PubMed AbstractThermorubin (THB) is a long-known broad-spectrum ribosome-targeting antibiotic, but the molecular mechanism of its action was unclear. Here, our precise fast-kinetics assays in a reconstituted ...Thermorubin (THB) is a long-known broad-spectrum ribosome-targeting antibiotic, but the molecular mechanism of its action was unclear. Here, our precise fast-kinetics assays in a reconstituted Escherichia coli translation system and 1.96 Å resolution cryo-EM structure of THB-bound 70S ribosome with mRNA and initiator tRNA, independently suggest that THB binding at the intersubunit bridge B2a near decoding center of the ribosome interferes with the binding of A-site substrates aminoacyl-tRNAs and class-I release factors, thereby inhibiting elongation and termination steps of bacterial translation. Furthermore, THB acts as an anti-dissociation agent that tethers the ribosomal subunits and blocks ribosome recycling, subsequently reducing the pool of active ribosomes. Our results show that THB does not inhibit translation initiation as proposed earlier and provide a complete mechanism of how THB perturbs bacterial protein synthesis. This in-depth characterization will hopefully spur efforts toward the design of THB analogs with improved solubility and effectivity against multidrug-resistant bacteria.
External linksNat Commun / PubMed:36806263 / PubMed Central
MethodsEM (single particle)
Resolution1.96 Å
Structure data

15712

8aye

EMDB-15712, PDB-8aye:
E. coli 70S ribosome bound to thermorubin and fMet-tRNA
Method: EM (single particle) / Resolution: 1.96 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-T8B:
Thermorubin

Source
  • escherichia coli (E. coli)
KeywordsRIBOSOME / Antibiotic / Initiator tRNA / Complex / Macromolecule

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