ArticleJournal of bacteriology2015
Modulation of decoding fidelity by ribosomal proteins S4 and S5.
Article in Journal of bacteriology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 35 citations in OpenAlex.
- Error-prone translation as a driver of proteostasis collapse and neurodegeneration.Neural regeneration research · 2026Article
- Structural adaptations for enhanced translation kinetics in evolved ribosomes.Nucleic acids research · 2026Article
- Multiscale Modeling of the Bacterial Ribosome to Identify Potential Peptide Modulators and Their Allosteric Effects.Biochemistry · 2026Article
- Epistasis and co-adaptation in bacterial genome evolution.Nature reviews. Genetics · 2026Review
- Interplay of the ribosome A and CAR sites.NAR genomics and bioinformatics · 2026Article
- Structural adaptations for enhanced translation kinetics in evolved ribosomes.bioRxiv : the preprint server for biology · 2026Article
- Mutations in ribosomal protein uS5 alter translation fidelity and mutagenesis inJournal of bacteriology · 2025Article
- Cost of Altered Translation Accuracy Shapes Adaptation to Antibiotics in E. coli.Molecular biology and evolution · 2025Article
- Efficient genetic code expansion without host genome modifications.Nature biotechnology · 2025Article
- Bacterial ribosome heterogeneity facilitates rapid response to stress.Journal of bacteriology · 2025Review
- The influence of downstream structured elements within mRNA on the dynamics of intersubunit rotation in ribosomes.RNA (New York, N.Y.) · 2025Article
- RsmG methylation of 16S rRNA affects the function of ribosomal protein uS12.Archives of microbiology · 2025Article
- Fluorescent reporters give new insights into antibiotics-induced nonsense and frameshift mistranslation.Scientific reports · 2024Article
- Extraribosomal Functions of Bacterial Ribosomal Proteins-An Update, 2023.International journal of molecular sciences · 2024Review
- The RNA-Binding Function of Ribosomal Proteins and Ribosome Biogenesis Factors in Human Health and Disease.Biomedicines · 2023Review
- Ribosomal Protein uS5 and Friends: Protein-Protein Interactions Involved in Ribosome Assembly and Beyond.Biomolecules · 2023Review
- Mapping the in vivo fitness landscape of a tethered ribosome.Science advances · 2023Article
- Translational Fidelity during Bacterial Stresses and Host Interactions.Pathogens (Basel, Switzerland) · 2023Review
- Directed evolution of rRNA improves translation kinetics and recombinant protein yield.Nature communications · 2021Article
- Fail-safe genetic codes designed to intrinsically contain engineered organisms.Nucleic acids research · 2019Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Ribosomal proteins S4 and S5 participate in the decoding and assembly processes on the ribosome and the interaction with specific antibiotic inhibitors of translation. Many of the characterized mutations affecting these proteins decrease the accuracy of translation, leading to a ribosomal-ambiguity phenotype. Structural analyses of ribosomal complexes indicate that the tRNA selection pathway involves a transition between the closed and open conformations of the 30S ribosomal subunit and requires disruption of the interface between the S4 and S5 proteins. In agreement with this observation, several of the mutations that promote miscoding alter residues located at the S4-S5 interface. Here, the Escherichia coli rpsD and rpsE genes encoding the S4 and S5 proteins were targeted for mutagenesis and screened for accuracy-altering mutations. While a majority of the 38 mutant proteins recovered decrease the accuracy of translation, error-restrictive mutations were also recovered; only a minority of the mutant proteins affected rRNA processing, ribosome assembly, or interactions with antibiotics. Several of the mutations affect residues at the S4-S5 interface. These include five nonsense mutations that generate C-terminal truncations of S4. These truncations are predicted to destabilize the S4-S5 interface and, consistent with the domain closure model, all have ribosomal-ambiguity phenotypes. A substantial number of the mutations alter distant locations and conceivably affect tRNA selection through indirect effects on the S4-S5 interface or by altering interactions with adjacent ribosomal proteins and 16S rRNA.
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Registered trials
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.