ArticlemBio2022
Structural Studies Reveal the Role of Helix 68 in the Elongation Step of Protein Biosynthesis.
Article in mBio, 2022. 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, 13 citations in OpenAlex.
- A small nucleolar RNA dictates the structure and function of translating ribosomes in Leishmania.Nature communications · 2026Article
- Peptide Nucleic Acids (PNAs) in Antimicrobial Therapy: A Next Generation Strategy.International journal of molecular sciences · 2026Review
- Ultrathin liquid cells for microsecond time-resolved cryo-EM.Nature communications · 2026Article
- Mechanistic insights intobioRxiv : the preprint server for biology · 2026Article
- Structural studies of ribosome from an anaerobic Bacteroidetes human pathogen Porphyromonas gingivalis.Nucleic acids research · 2025Article
- Ribosomes: from conserved origin to functional/medical mobility and heterogeneity.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Review
- YjgA plays dual roles in enhancing PTC maturation.Nucleic acids research · 2024Article
- Ribosome Pool Engineering Increases Protein Biosynthesis Yields.ACS central science · 2024Article
- The structure of a hibernating ribosome in a Lyme disease pathogen.Nature communications · 2023Article
- Cryo-electron microscopy structure and translocation mechanism of the crenarchaeal ribosome.Nucleic acids research · 2023Article
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
Abstract
The ribosome, a multicomponent assembly consisting of RNA and proteins, is a pivotal macromolecular machine that translates the genetic code into proteins. The large ribosomal subunit rRNA helix 68 (H68) is a key element in the protein synthesis process, as it coordinates the coupled movements of the actors involved in translocation, including the tRNAs and L1 stalk. Examination of cryo-electron microscopy (cryo-EM) structures of ribosomes incubated for various time durations at physiological temperatures led to the identification of functionally relevant H68 movements. These movements assist the transition of the L1 stalk between its open and closed states. H68 spatial flexibility and its significance to the protein synthesis process were confirmed through its effective targeting with antisense PNA oligomers. Our results suggest that H68 is actively involved in ribosome movements that are central to the elongation process.
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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 OpenQuestion graph.