ArticleProceedings of the National Academy of Sciences of the United States of America2008
Crystal structure of a translation termination complex formed with release factor RF2.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 144 papers.
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Who cites it
144 citing papers in PubMed, 255 citations in OpenAlex.
- RNAViruses · 2026Review
- A cascade of structural rearrangements positions peptide release factor 2 for polypeptide hydrolysis on the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Mechanism of release factor-mediated peptidyl-tRNA hydrolysis on the ribosome.Science (New York, N.Y.) · 2025Article
- A mini-hairpin shaped nascent peptide blocks translation termination by a distinct mechanism.Nature communications · 2025Article
- Article
- Marked Genome Reduction Driven by a Parasitic Lifestyle: Two Complete Genomes of Endosymbiotic Bacteria Possibly Hosted by a Dinoflagellate.Microbes and environments · 2025Article
- Developing Multichannel smFRET Approach to Dissecting Ribosomal Mechanisms.Chemical & biomedical imaging · 2024Article
- The eRF1 degrader SRI-41315 acts as a molecular glue at the ribosomal decoding center.Nature chemical biology · 2024Article
- SnoRNAs: Exploring Their Implication in Human Diseases.International journal of molecular sciences · 2024Review
- Structural basis of translation inhibition by a valine tRNA-derived fragment.Life science alliance · 2024Article
- Decoding the Enigma: Translation Termination in Human Mitochondria.Human molecular genetics · 2024Review
- Article
- Molecular basis of the pleiotropic effects by the antibiotic amikacin on the ribosome.Nature communications · 2023Article
- Dynamics of release factor recycling during translation termination in bacteria.Nucleic acids research · 2023Article
- Molecular size dependence on achievable resolution from XFEL single-particle 3D reconstruction.Structural dynamics (Melville, N.Y.) · 2023Article
- Noncanonical amino acid mutagenesis in response to recoding signal-enhanced quadruplet codons.Nucleic acids research · 2022Article
- Hyper-swivel head domain motions are required for complete mRNA-tRNA translocation and ribosome resetting.Nucleic acids research · 2022Article
- The universally conserved nucleotides of the small subunit ribosomal RNAs.RNA (New York, N.Y.) · 2022Article
- Bacterial Ribosome Rescue Systems.Microorganisms · 2022Review
- Maintaining mitochondrial ribosome function: The role of ribosome rescue and recycling factors.RNA biology · 2022Review
84 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We report the crystal structure of a translation termination complex formed by the Thermus thermophilus 70S ribosome bound with release factor RF2, in response to a UAA stop codon, solved at 3 A resolution. The backbone of helix alpha5 and the side chain of serine of the conserved SPF motif of RF2 recognize U1 and A2 of the stop codon, respectively. A3 is unstacked from the first 2 bases, contacting Thr-216 and Val-203 of RF2 and stacking on G530 of 16S rRNA. The structure of the RF2 complex supports our previous proposal that conformational changes in the ribosome in response to recognition of the stop codon stabilize rearrangement of the switch loop of the release factor, resulting in docking of the universally conserved GGQ motif in the PTC of the 50S subunit. As seen for the RF1 complex, the main-chain amide nitrogen of glutamine in the GGQ motif is positioned to contribute directly to catalysis of peptidyl-tRNA hydrolysis, consistent with mutational studies, which show that most side-chain substitutions of the conserved glutamine have little effect. We show that when the H-bonding capability of the main-chain N-H of the conserved glutamine is eliminated by substitution with proline, peptidyl-tRNA esterase activity is abolished, consistent with its proposed role in catalysis.
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