ArticleProceedings of the National Academy of Sciences of the United States of America2013
Reorganization of an intersubunit bridge induced by disparate 16S ribosomal ambiguity mutations mimics an EF-Tu-bound state.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- RNAViruses · 2026Review
- Multiscale Modeling of the Bacterial Ribosome to Identify Potential Peptide Modulators and Their Allosteric Effects.Biochemistry · 2026Article
- Human protein synthesis requires aminoacyl-tRNA pivoting during proofreading.Nature communications · 2025Article
- Geometric alignment of aminoacyl-tRNA relative to catalytic centers of the ribosome underpins accurate mRNA decoding.Nature communications · 2023Article
- Ratchet, swivel, tilt and roll: a complete description of subunit rotation in the ribosome.Nucleic acids research · 2023Article
- In vitro evaluation of gentamicin activity against Spanish field isolates of Brachyspira hyodysenteriae.Porcine health management · 2022Article
- Regulation of translation by site-specific ribosomal RNA methylation.Nature structural & molecular biology · 2021Article
- The case of the missing allosteric ribozymes.Nature chemical biology · 2021Review
- Importance of a tRNA anticodon loop modification and a conserved, noncanonical anticodon stem pairing inThe Journal of biological chemistry · 2019Article
- Ribosomal ambiguity (ram) mutations promote the open (off) to closed (on) transition and thereby increase miscoding.Nucleic acids research · 2019Article
- RNA Structural Dynamics As Captured by Molecular Simulations: A Comprehensive Overview.Chemical reviews · 2018Review
- Exploring allosteric communication in multiple states of the bacterial ribosome using residue network analysis.Turkish journal of biology = Turk biyoloji dergisi · 2018Article
- Matrine derivate MASM uncovers a novel function for ribosomal protein S5 in osteoclastogenesis and postmenopausal osteoporosis.Cell death & disease · 2017Article
- In-Culture Cross-Linking of Bacterial Cells Reveals Large-Scale Dynamic Protein-Protein Interactions at the Peptide Level.Journal of proteome research · 2017Article
- Mistakes in translation: Reflections on mechanism.PloS one · 2017Article
- Intersubunit Bridges of the Bacterial Ribosome.Journal of molecular biology · 2016Review
- Epistasis analysis of 16S rRNA ram mutations helps define the conformational dynamics of the ribosome that influence decoding.RNA (New York, N.Y.) · 2016Article
- Dynamic contact network between ribosomal subunits enables rapid large-scale rotation during spontaneous translocation.Nucleic acids research · 2015Article
- Modulation of decoding fidelity by ribosomal proteins S4 and S5.Journal of bacteriology · 2015Article
- Another look at mutations in ribosomal protein S4 lends strong support to the domain closure model.Journal of bacteriology · 2015Article
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Abstract
After four decades of research aimed at understanding tRNA selection on the ribosome, the mechanism by which ribosomal ambiguity (ram) mutations promote miscoding remains unclear. Here, we present two X-ray crystal structures of the Thermus thermophilus 70S ribosome containing 16S rRNA ram mutations, G347U and G299A. Each of these mutations causes miscoding in vivo and stimulates elongation factor thermo unstable (EF-Tu)-dependent GTP hydrolysis in vitro. Mutation G299A is located near the interface of ribosomal proteins S4 and S5 on the solvent side of the subunit, whereas G347U is located 77 Å distant, at intersubunit bridge B8, close to where EF-Tu engages the ribosome. Despite these disparate locations, both mutations induce almost identical structural rearrangements that disrupt the B8 bridge--namely, the interaction of h8/h14 with L14 and L19. This conformation most closely resembles that seen upon EF-Tu-GTP-aminoacyl-tRNA binding to the 70S ribosome. These data provide evidence that disruption and/or distortion of B8 is an important aspect of GTPase activation. We propose that, by destabilizing B8, G299A and G347U reduce the energetic cost of attaining the GTPase-activated state and thereby decrease the stringency of decoding. This previously unappreciated role for B8 in controlling the decoding process may hold relevance for many other ribosomal mutations known to influence translational fidelity.
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