ArticleNucleic acids research2018
Conformational switch in the ribosomal protein S1 guides unfolding of structured RNAs for translation initiation.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 16 citations in OpenAlex.
- Extraribosomal Functions of Bacterial Ribosomal Proteins-An Update, 2023.International journal of molecular sciences · 2024Review
- Cell-free transcription-translation system: a dual read-out assay to characterize riboswitch function.Nucleic acids research · 2023Article
- Article
- Bacterial RNA chaperones and chaperone-like riboregulators: behind the scenes of RNA-mediated regulation of cellular metabolism.RNA biology · 2022Article
- Switching at the ribosome: riboswitches need rProteins as modulators to regulate translation.Nature communications · 2021Article
- NMR structure of the Vibrio vulnificus ribosomal protein S1 domains D3 and D4 provides insights into molecular recognition of single-stranded RNAs.Nucleic acids research · 2021Article
- Identification of Amyloidogenic Regions inInternational journal of molecular sciences · 2021Article
- An RNA pseudoknot is essential for standby-mediated translation of the tisB toxin mRNA in Escherichia coli.Nucleic acids research · 2020Article
- Translation inhibition from a distance: The small RNA SgrS silences a ribosomal protein S1-dependent enhancer.Molecular microbiology · 2020Article
- Protein unties the pseudoknot: S1-mediated unfolding of RNA higher order structure.Nucleic acids research · 2020Article
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5 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Initiation of bacterial translation requires that the ribosome-binding site in mRNAs adopts single-stranded conformations. In Gram-negative bacteria the ribosomal protein S1 (rS1) is a key player in resolving of structured elements in mRNAs. However, the exact mechanism of how rS1 unfolds persistent secondary structures in the translation initiation region (TIR) is still unknown. Here, we show by NMR spectroscopy that Vibrio vulnificus rS1 displays a unique architecture of its mRNA-binding domains, where domains D3 and D4 provide the mRNA-binding platform and cover the nucleotide binding length of the full-length rS1. D5 significantly increases rS1's chaperone activity, although it displays structural heterogeneity both in isolation and in presence of the other domains, albeit to varying degrees. The heterogeneity is induced by the switch between the two equilibrium conformations and is triggered by an order-to-order transition of two mutually exclusive secondary structures (β-strand-to-α-helix) of the 'AERERI' sequence. The conformational switching is exploited for melting of structured 5'-UTR's, as the conformational heterogeneity of D5 can compensate the entropic penalty of complex formation. Our data thus provides a detailed understanding of the intricate coupling of protein and RNA folding dynamics enabling translation initiation of structured mRNAs.
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