ArticleJournal of molecular biology2009
Global stabilization of rRNA structure by ribosomal proteins S4, S17, and S20.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- A comprehensive view on r-protein binding and rRNA domain structuring during early eukaryotic ribosome formation.Nucleic acids research · 2026Article
- Regulation of Hindbrain Vascular Development byCells · 2025Article
- Structurally heterogeneous ribosomes cooperate in protein synthesis in bacterial cells.Nature communications · 2025Article
- Disassembly of unstable RNA structures by an E. coli DEAD-box chaperone accelerates ribosome assembly.Nucleic acids research · 2025Article
- Mitochondrial RNA in Inflammation.International journal of biological sciences · 2025Review
- Ribosomal Protein S12 Hastens Nucleation of Co-Transcriptional Ribosome Assembly.Biomolecules · 2023Article
- Review
- Comparative Analysis of Structural and Dynamical Features of Ribosome Upon Association With mRNA Reveals Potential Role of Ribosomal Proteins.Frontiers in molecular biosciences · 2021Article
- RsmG forms stable complexes with premature small subunit rRNA during bacterial ribosome biogenesis.RSC advances · 2020Article
- Pseudouridine Synthase RsuA Captures an Assembly Intermediate that Is Stabilized by Ribosomal Protein S17.Biomolecules · 2020Article
- Genetic ablation of the mitoribosome in the malaria parasiteThe Journal of biological chemistry · 2020Article
- Posttranscriptional Regulation ofJournal of bacteriology · 2020Article
- Article
- Evolution of protein-coupled RNA dynamics during hierarchical assembly of ribosomal complexes.Nature communications · 2017Article
- Ribosomal DNA copy number amplification and loss in human cancers is linked to tumor genetic context, nucleolus activity, and proliferation.PLoS genetics · 2017Article
- The C-terminus of ribosomal protein uS4 contributes to small ribosomal subunit biogenesis and the fidelity of translation.Biochimie · 2017Article
- Compensating the Fitness Costs of Synonymous Mutations.Molecular biology and evolution · 2016Article
- Differential effects of ribosomal proteins and Mg2+ ions on a conformational switch during 30S ribosome 5'-domain assembly.RNA (New York, N.Y.) · 2015Article
- Assembly constraints drive co-evolution among ribosomal constituents.Nucleic acids research · 2015Article
- Deletion of L4 domains reveals insights into the importance of ribosomal protein extensions in eukaryotic ribosome assembly.RNA (New York, N.Y.) · 2014Article
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2 authors.
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Abstract
Ribosomal proteins stabilize the folded structure of the ribosomal RNA and enable the recruitment of further proteins to the complex. Quantitative hydroxyl radical footprinting was used to measure the extent to which three different primary assembly proteins, S4, S17, and S20, stabilize the three-dimensional structure of the Escherichia coli 16S 5' domain. The stability of the complexes was perturbed by varying the concentration of MgCl(2). Each protein influences the stability of the ribosomal RNA tertiary interactions beyond its immediate binding site. S4 and S17 stabilize the entire 5' domain, while S20 has a more local effect. Multistage folding of individual helices within the 5' domain shows that each protein stabilizes a different ensemble of structural intermediates that include nonnative interactions at low Mg(2+) concentration. We propose that the combined interactions of S4, S17, and S20 with different helical junctions bias the free-energy landscape toward a few RNA conformations that are competent to add the secondary assembly protein S16 in the next step of assembly.
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