ArticleMolecular cell2025
The RNA helicase HrpA rescues collided ribosomes in E. coli.
Article in Molecular cell, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed.
- Collided ribosomes are rescued by the endonuclease Rae1 andbioRxiv : the preprint server for biology · 2026Article
- Blocked transcription-translation complexes are rescued by transcript release followed byJournal of bacteriology · 2026Article
- The alarmone pGpp inhibits translation through GTP depletion.Nucleic acids research · 2026Article
- Synthesis of Ultra-Large Fibrous Proteins from Bacteria via a Looped-Translation System.bioRxiv : the preprint server for biology · 2026Article
- Mechanism of RACK1-dependent ZAKα activation at stalled and collided ribosomes.Molecular cell · 2026Article
- Starvation-independent alarmone production inhibits translation through GTP depletion.bioRxiv : the preprint server for biology · 2026Article
- Translation quality control in Pseudomonas aeruginosa: current knowledge and perspectives.FEMS microbiology reviews · 2026Review
- Structural and functional perspectives on DEAD-box RNA helicases in the rubber tree cold stress response.Frontiers in plant science · 2026Review
- Combined transcriptome and metabolome analysis reveals the regulatory network of histidine kinase QseC in the two-component system ofFrontiers in microbiology · 2025Article
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Abstract
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.
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