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TitleThe RNA helicase HrpA rescues collided ribosomes in E. coli.
Journal, issue, pagesMol Cell, Vol. 85, Issue 5, Page 999-1007.e7, Year 2025
Publish dateMar 6, 2025
AuthorsAnnabelle Campbell / Hanna F Esser / A Maxwell Burroughs / Otto Berninghausen / L Aravind / Thomas Becker / Rachel Green / Roland Beckmann / Allen R Buskirk /
PubMed AbstractAlthough many antibiotics inhibit bacterial ribosomes, the loss of known factors that rescue stalled ribosomes does not lead to robust antibiotic sensitivity in E. coli, suggesting the existence of ...Although many antibiotics inhibit bacterial ribosomes, the loss of known factors that rescue stalled ribosomes does not lead to robust antibiotic sensitivity in E. coli, suggesting the existence of additional mechanisms. Here, we show that the RNA helicase HrpA rescues stalled ribosomes in E. coli. Acting selectively on ribosomes that have collided, HrpA uses ATP hydrolysis to split stalled ribosomes into subunits. Cryoelectron microscopy (cryo-EM) structures reveal how HrpA simultaneously binds to two collided ribosomes, explaining its selectivity, and how its helicase module engages downstream mRNA such that, by exerting a pulling force on the mRNA, it would destabilize the stalled ribosome. These studies show that ribosome splitting is a conserved mechanism that allows proteobacteria to tolerate ribosome-targeting antibiotics.
External linksMol Cell / PubMed:39922193 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 3.2 Å
Structure data

51318

9gft

EMDB-51318, PDB-9gft:
Structure of the HrpA-bound E. coli disome, Class I
Method: EM (single particle) / Resolution: 3.1 Å

51340

9ggr

EMDB-51340, PDB-9ggr:
Structure of the HrpA-bound E. coli disome, Class II
Method: EM (single particle) / Resolution: 3.2 Å

Source
  • escherichia coli (E. coli)
  • vibrio alginolyticus (bacteria)
KeywordsRIBOSOME / RNA helicase

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