ArticlePLoS biology2013
Escherichia coli ribosomal protein S1 unfolds structured mRNAs onto the ribosome for active translation initiation.
Article in PLoS biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.
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Who cites it
99 citing papers in PubMed, 181 citations in OpenAlex.
- Structure of a specialized 70S initiation complex.Nucleic acids research · 2026Article
- Stoichiometry-induced differential selection on codon optimization among ribosomal protein genes in bacterial species.Molecular biology and evolution · 2026Article
- Extended Shine-Dalgarno motifs govern translation initiation in Staphylococcus aureus.Nature communications · 2026Article
- Structure and mechanism of antiphage retron Eco2.Nature structural & molecular biology · 2026Article
- Structure of the 30S translation initiation complex coupled to paused RNA polymerase and its potential for riboregulation.Nature communications · 2025Article
- Base composition at the start of the coding sequence controls the balance between translation initiation and mRNA degradation in E. coli.Nucleic acids research · 2025Article
- The knowledge driven DBTL cycle provides mechanistic insights while optimising dopamine production in Escherichia coli.Microbial cell factories · 2025Article
- Reversible acetylation of ribosomal protein S1 serves as a smart switch for Salmonella to rapidly adapt to host stress.Nucleic acids research · 2025Article
- Molecular basis of mRNA delivery to the bacterial ribosome.Science (New York, N.Y.) · 2024Article
- Cooperation of regulatory RNA and the RNA degradosome in transcript surveillance.Nucleic acids research · 2024Article
- Disentangling the pseudoknots of toxin translation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Bactericidal effect of tetracycline in E. coli strain ED1a may be associated with ribosome dysfunction.Nature communications · 2024Article
- Extraribosomal Functions of Bacterial Ribosomal Proteins-An Update, 2023.International journal of molecular sciences · 2024Review
- The BR-body proteome contains a complex network of protein-protein and protein-RNA interactions.Cell reports · 2023Article
- The P-Site Loop of the Universally Conserved Bacterial Ribosomal Protein L5 Is Required for Maintaining Both Translation Rate and Fidelity.International journal of molecular sciences · 2023Article
- The BR-body proteome contains a complex network of protein-protein and protein-RNA interactions.bioRxiv : the preprint server for biology · 2023Article
- Perturbation of protein homeostasis brings plastids at the crossroad between repair and dismantling.PLoS genetics · 2023Article
- Structural insights into the binding of bS1 to the ribosome.Nucleic acids research · 2023Article
- Proteomic Profiling Reveals Cytotoxic Mechanisms of Action and Adaptive Mechanisms of Resistance inACS omega · 2023Article
- Hfq protein and GcvB small RNA tailoring ofRNA biology · 2023Article
39 more citing papers are in PubMed but not listed here.
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Authors and funding
12 authors at 8 institutions in 3 countries.
Funding
Abstract
Regulation of translation initiation is well appropriate to adapt cell growth in response to stress and environmental changes. Many bacterial mRNAs adopt structures in their 5' untranslated regions that modulate the accessibility of the 30S ribosomal subunit. Structured mRNAs interact with the 30S in a two-step process where the docking of a folded mRNA precedes an accommodation step. Here, we used a combination of experimental approaches in vitro (kinetic of mRNA unfolding and binding experiments to analyze mRNA-protein or mRNA-ribosome complexes, toeprinting assays to follow the formation of ribosomal initiation complexes) and in vivo (genetic) to monitor the action of ribosomal protein S1 on the initiation of structured and regulated mRNAs. We demonstrate that r-protein S1 endows the 30S with an RNA chaperone activity that is essential for the docking and the unfolding of structured mRNAs, and for the correct positioning of the initiation codon inside the decoding channel. The first three OB-fold domains of S1 retain all its activities (mRNA and 30S binding, RNA melting activity) on the 30S subunit. S1 is not required for all mRNAs and acts differently on mRNAs according to the signals present at their 5' ends. This work shows that S1 confers to the ribosome dynamic properties to initiate translation of a large set of mRNAs with diverse structural features.
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