ArticleNucleic acids research2023
Insights into translocation mechanism and ribosome evolution from cryo-EM structures of translocation intermediates of Giardia intestinalis.
Article in Nucleic acids research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- Cryo-EM structure of ribosome from pathogenic protozoa Entamoeba histolytica reveals unique features of its architecture.Nature communications · 2025Article
- Multi-channel smFRET study reveals a compact conformation of EF-G on the ribosome.The international journal of biochemistry & cell biology · 2025Article
- Evolutionary insights into elongation factor G using AlphaFold and ancestral analysis.Computers in biology and medicine · 2025Article
- Review
- Capturing eukaryotic ribosome dynamics in situ at high resolution.Nature structural & molecular biology · 2025Article
- Allosteric Effects of EF-G Domain I Mutations Inducing Ribosome Frameshifting Revealed by Multiplexed Force Spectroscopy.Chembiochem : a European journal of chemical biology · 2024Article
- The Giardia lamblia ribosome structure reveals divergence in several biological pathways and the mode of emetine function.Structure (London, England : 1993) · 2024Article
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6 authors at 1 institution in 1 country.
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Abstract
Giardia intestinalis is a protozoan parasite that causes diarrhea in humans. Using single-particle cryo-electron microscopy, we have determined high-resolution structures of six naturally populated translocation intermediates, from ribosomes isolated directly from actively growing Giardia cells. The highly compact and uniquely GC-rich Giardia ribosomes possess eukaryotic rRNAs and ribosomal proteins, but retain some bacterial features. The translocation intermediates, with naturally bound tRNAs and eukaryotic elongation factor 2 (eEF2), display characteristic ribosomal intersubunit rotation and small subunit's head swiveling-universal for translocation. In addition, we observe the eukaryote-specific 'subunit rolling' dynamics, albeit with limited features. Finally, the eEF2·GDP state features a uniquely positioned 'leaving phosphate (Pi)' that proposes hitherto unknown molecular events of Pi and eEF2 release from the ribosome at the final stage of translocation. In summary, our study elucidates the mechanism of translocation in the protists and illustrates evolution of the translation machinery from bacteria to eukaryotes from both the structural and mechanistic perspectives.
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