ArticleNature communications2024
Transient disome complex formation in native polysomes during ongoing protein synthesis captured by cryo-EM.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Article
- Article
- A Microscale Platform for the Comprehensive Analysis of Bacterial Translation Initiation.International journal of molecular sciences · 2026Article
- Visualizing the translation landscape in human cells at high resolution.Nature communications · 2025Article
- The RNA helicase HrpA rescues collided ribosomes in E. coli.Molecular cell · 2025Article
- Novel archaeal ribosome dimerization factor facilitating unique 30S-30S dimerization.Nucleic acids research · 2025Article
- The RNA helicase HrpA rescues collided ribosomes inbioRxiv : the preprint server for biology · 2024Article
- Comprehensive translational profiling and STE AI uncover rapid control of protein biosynthesis during cell stress.Nucleic acids research · 2024Article
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
Abstract
Structural studies of translating ribosomes traditionally rely on in vitro assembly and stalling of ribosomes in defined states. To comprehensively visualize bacterial translation, we reactivated ex vivo-derived E. coli polysomes in the PURE in vitro translation system and analyzed the actively elongating polysomes by cryo-EM. We find that 31% of 70S ribosomes assemble into disome complexes that represent eight distinct functional states including decoding and termination intermediates, and a pre-nucleophilic attack state. The functional diversity of disome complexes together with RNase digest experiments suggests that paused disome complexes transiently form during ongoing elongation. Structural analysis revealed five disome interfaces between leading and queueing ribosomes that undergo rearrangements as the leading ribosome traverses through the elongation cycle. Our findings reveal at the molecular level how bL9's CTD obstructs the factor binding site of queueing ribosomes to thwart harmful collisions and illustrate how translation dynamics reshape inter-ribosomal contacts.
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