ArticleStructure (London, England : 1993)2022
CryoEM structures of pseudouridine-free ribosome suggest impacts of chemical modifications on ribosome conformations.
Article in Structure (London, England : 1993), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 36 citations in OpenAlex.
- Structural basis for emetine inhibition of ribosome translocation inbioRxiv : the preprint server for biology · 2026Article
- Cryo-EM structure of the naked mole-rat ribosome reveals a stabilized split 28S rRNA.Nature communications · 2026Article
- Nanopore Sequencing Reveals rRNA Modification Changes in Human Cells Experiencing Oxidative or Inflammatory Stress.ACS chemical biology · 2026Article
- 2'-O-Methylation maintains ribosome structural and translation integrity.Molecular cell · 2026Article
- Ribosomal modifications are associated with mesenchymal fate selection in the neural crest lineage.Nature communications · 2026Article
- Mechanistic insight into the pseudouridylation of RNA.RNA biology · 2025Review
- Pseudouridine increases ribosome stability in a thermophilic eukaryote.Nucleic acids research · 2025Article
- Functions and therapeutic applications of pseudouridylation.Nature reviews. Molecular cell biology · 2025Review
- Structural basis for hygromycin B inhibition of yeast pseudouridine-deficient ribosomes.Science advances · 2025Article
- Ribosomes: from conserved origin to functional/medical mobility and heterogeneity.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Review
- The zebrafish (NAR genomics and bioinformatics · 2025Article
- Human tumor suppressor protein Pdcd4 binds at the mRNA entry channel in the 40S small ribosomal subunit.Nature communications · 2024Article
- The structure of the human 80S ribosome at 1.9 Å resolution reveals the molecular role of chemical modifications and ions in RNA.Nature structural & molecular biology · 2024Article
- Structural and mechanistic insights into the function of Leishmania ribosome lacking a single pseudouridine modification.Cell reports · 2024Article
- Cryo-EM structure of wheat ribosome reveals unique features of the plant ribosomes.Structure (London, England : 1993) · 2024Article
- Comprehensive map of ribosomal 2'-O-methylation and C/D box snoRNAs in Drosophila melanogaster.Nucleic acids research · 2024Article
- Implication of Stm1 in the protection of eIF5A, eEF2 and tRNA through dormant ribosomes.Frontiers in molecular biosciences · 2024Article
- A single pseudouridine on rRNA regulates ribosome structure and function in the mammalian parasite Trypanosoma brucei.Nature communications · 2023Article
- Regulation of translation by ribosomal RNA pseudouridylation.Science advances · 2023Article
- How does precursor RNA structure influence RNA processing and gene expression?Bioscience reports · 2023Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Pseudouridine, the most abundant form of RNA modification, is known to play important roles in ribosome function. Mutations in human DKC1, the pseudouridine synthase responsible for catalyzing the ribosome RNA modification, cause translation deficiencies and are associated with a complex cancer predisposition. The structural basis for how pseudouridine impacts ribosome function remains uncharacterized. Here, we characterized structures and conformations of a fully modified and a pseudouridine-free ribosome from Saccharomyces cerevisiae in the absence of ligands or when bound with translocation inhibitor cycloheximide by electron cryomicroscopy. In the modified ribosome, the rearranged N1 atom of pseudouridine is observed to stabilize key functional motifs by establishing predominately water-mediated close contacts with the phosphate backbone. The pseudouridine-free ribosome, however, is devoid of such interactions and displays conformations reflective of abnormal inter-subunit movements. The erroneous motions of the pseudouridine-free ribosome may explain its observed deficiencies in translation.
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