ArticleProceedings of the National Academy of Sciences of the United States of America2020
Direct visualization of translational GTPase factor pool formed around the archaeal ribosomal P-stalk by high-speed AFM.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. 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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21 citing papers in PubMed, 91 citations in OpenAlex.
- Regulatory dynamics of monosomes and polysomes in cellular adaptation.Journal of biochemistry · 2026Review
- Ribosomal allostery as a potential regulator of bacterial dormancy.Nature communications · 2026Article
- Discovery and mutasynthetic optimization of ansatrienin B: A new broad-spectrum inhibitor against RNA viruses.Acta pharmaceutica Sinica. B · 2026Article
- Feedforward compensation of piezo nonlinearity for high-precision high-speed atomic force microscopy.Scientific reports · 2026Article
- Structural Dynamics of the Afamin/Wnt3a Complex Mediated by the Afamin Hydrophobic Pocket.Nano letters · 2026Article
- Multivalent Interactions between Chaperone and Ribosome-Nascent Chain Complex Revealed by High-Speed AFM and MD Simulations.ACS nano · 2025Article
- Near-cognate tRNAs enhance tRNA rejection and prime the ribosome for rapid subsequent tRNA testing.Biophysical journal · 2025Article
- Ribosomal L12 stalks recruit elongation factors to speed protein synthesis in Escherichia coli.Communications biology · 2025Article
- Specialized ribosomes: integrating new insights and current challenges.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Review
- Single-Molecule Studies of Cognate and Near-Cognate Elongation in anbioRxiv : the preprint server for biology · 2024Article
- Structure-Function Analysis of the A1 Subunit of Shiga Toxin 2 with Peptides That Target the P-Stalk Binding Site and Inhibit Activity.Biochemistry · 2024Article
- Simulating biological surface dynamics in high-speed atomic force microscopy experiments.Biophysical reviews · 2023Article
- CryoEM reveals that ribosomes in microsporidian spores are locked in a dimeric hibernating state.Nature microbiology · 2023Article
- Simultaneous measurement of nascent transcriptome and translatome using 4-thiouridine metabolic RNA labeling and translating ribosome affinity purification.Nucleic acids research · 2023Article
- Spatiotemporal resolution in high-speed atomic force microscopy for studying biological macromolecules in action.Microscopy (Oxford, England) · 2023Review
- Archaea/eukaryote-specific ribosomal proteins - guardians of a complex structure.Computational and structural biotechnology journal · 2023Review
- Functional Implications of Dynamic Structures of Intrinsically Disordered Proteins Revealed by High-Speed AFM Imaging.Biomolecules · 2022Review
- The flexible N-terminal motif of uL11 unique to eukaryotic ribosomes interacts with P-complex and facilitates protein translation.Nucleic acids research · 2022Article
- Ambient Temperature Stable, Scalable COVID-19 Polymer Particle Vaccines Induce Protective Immunity.Advanced healthcare materials · 2022Article
- Distinct mechanisms of the human mitoribosome recycling and antibiotic resistance.Nature communications · 2021Article
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3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In translation elongation, two translational guanosine triphosphatase (trGTPase) factors EF1A and EF2 alternately bind to the ribosome and promote polypeptide elongation. The ribosomal stalk is a multimeric ribosomal protein complex which plays an essential role in the recruitment of EF1A and EF2 to the ribosome and their GTP hydrolysis for efficient and accurate translation elongation. However, due to the flexible nature of the ribosomal stalk, its structural dynamics and mechanism of action remain unclear. Here, we applied high-speed atomic force microscopy (HS-AFM) to directly visualize the action of the archaeal ribosomal heptameric stalk complex, aP0•(aP1•aP1)
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