ArticleStructure (London, England : 1993)2024
The Giardia lamblia ribosome structure reveals divergence in several biological pathways and the mode of emetine function.
Article in Structure (London, England : 1993), 2024. 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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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- Structural basis for emetine inhibition of ribosome translocation inbioRxiv : the preprint server for biology · 2026Article
- tRNA synthetase activity is required for stress granule and P-body assembly.Genes & development · 2026Article
- Cryo-EM structure of ribosome from pathogenic protozoa Entamoeba histolytica reveals unique features of its architecture.Nature communications · 2025Article
- Structure of an archaeal ribosome reveals a divergent active site and hibernation factor.Nature microbiology · 2025Article
- High-Throughput Repurposing Screen Reveals Compounds with Activity againstACS infectious diseases · 2025Article
- High-resolution reconstruction of aRNA (New York, N.Y.) · 2024Article
- High Throughput Repurposing Screen Reveals Compounds with Activity AgainstbioRxiv : the preprint server for biology · 2024Article
- Insights into translocation mechanism and ribosome evolution from cryo-EM structures of translocation intermediates of Giardia intestinalis.Nucleic acids research · 2023Article
- Precise gene models using long-read sequencing reveal a unique poly(A) signal inRNA (New York, N.Y.) · 2022Article
- Cryo-EM structure of the ancient eukaryotic ribosome from the human parasite Giardia lamblia.Nucleic acids research · 2022Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Giardia lamblia is a deeply branching protist and a human pathogen. Its unusual biology presents the opportunity to explore conserved and fundamental molecular mechanisms. We determined the structure of the G. lamblia 80S ribosome bound to tRNA, mRNA, and the antibiotic emetine by cryo-electron microscopy, to an overall resolution of 2.49 Å. The structure reveals rapidly evolving protein and nucleotide regions, differences in the peptide exit tunnel, and likely altered ribosome quality control pathways. Examination of translation initiation factor binding sites suggests these interactions are conserved despite a divergent initiation mechanism. Highlighting the potential of G. lamblia to resolve conserved biological principles; our structure reveals the interactions of the translation inhibitor emetine with the ribosome and mRNA, thus providing insight into the mechanism of action for this widely used antibiotic. Our work defines key questions in G. lamblia and motivates future experiments to explore the diversity of eukaryotic gene regulation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.