ArticleProceedings of the National Academy of Sciences of the United States of America2019
Spontaneous ribosomal translocation of mRNA and tRNAs into a chimeric hybrid state.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 52 citations in OpenAlex.
- Recoding by NNature communications · 2026Article
- Chinese cobra (Naja atra) SVPLACommunications biology · 2026Article
- The ribosome derives the energy to translocate and unwind mRNA from EF-G binding.Nature communications · 2025Article
- An RNA modification prevents extended codon-anticodon interactions from facilitating +1 frameshifting.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
- Implication of nucleotides near the 3' end of 16S rRNA in guarding the translational reading frame.Nucleic acids research · 2024Article
- The role of molecular chaperone CCT/TRiC in translation elongation: A literature review.Heliyon · 2024Review
- Cryo-electron microscopy structure and translocation mechanism of the crenarchaeal ribosome.Nucleic acids research · 2023Article
- A model for ribosome translocation based on the alternated displacement of its subunits.European biophysics journal : EBJ · 2023Article
- The role of GTP hydrolysis by EF-G in ribosomal translocation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Altered tRNA dynamics during translocation on slippery mRNA as determinant of spontaneous ribosome frameshifting.Nature communications · 2022Article
- The Structural Dynamics of Translation.Annual review of biochemistry · 2022Review
- Genome Expansion by tRNA +1 Frameshifting at Quadruplet Codons.Journal of molecular biology · 2022Review
- Genetic code degeneracy is established by the decoding center of the ribosome.Nucleic acids research · 2022Article
- Mechanisms of ribosome recycling in bacteria and mitochondria: a structural perspective.RNA biology · 2022Review
- Time-resolved cryo-EM visualizes ribosomal translocation with EF-G and GTP.Nature communications · 2021Article
- Weakening the IF2-fMet-tRNA Interaction Suppresses the Lethal Phenotype Caused by GTPase Inactivation.International journal of molecular sciences · 2021Article
- Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation.Nature communications · 2021Article
- From Recoding to Peptides for MHC Class I Immune Display: Enriching Viral Expression, Virus Vulnerability and Virus Evasion.Viruses · 2021Review
- Mechanisms and regulation of protein synthesis in mitochondria.Nature reviews. Molecular cell biology · 2021Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The elongation factor G (EF-G)-catalyzed translocation of mRNA and tRNA through the ribosome is essential for vacating the ribosomal A site for the next incoming aminoacyl-tRNA, while precisely maintaining the translational reading frame. Here, the 3.2-Å crystal structure of a ribosome translocation intermediate complex containing mRNA and two tRNAs, formed in the absence of EF-G or GTP, provides insight into the respective roles of EF-G and the ribosome in translocation. Unexpectedly, the head domain of the 30S subunit is rotated by 21°, creating a ribosomal conformation closely resembling the two-tRNA chimeric hybrid state that was previously observed only in the presence of bound EF-G. The two tRNAs have moved spontaneously from their A/A and P/P binding states into ap/P and pe/E states, in which their anticodon loops are bound between the 30S body domain and its rotated head domain, while their acceptor ends have moved fully into the 50S P and E sites, respectively. Remarkably, the A-site tRNA translocates fully into the classical P-site position. Although the mRNA also undergoes movement, codon-anticodon interaction is disrupted in the absence of EF-G, resulting in slippage of the translational reading frame. We conclude that, although movement of both tRNAs and mRNA (along with rotation of the 30S head domain) can occur in the absence of EF-G and GTP, EF-G is essential for enforcing coupled movement of the tRNAs and their mRNA codons to maintain the reading frame.
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