ArticleMethods (San Diego, Calif.)2018
Structural dynamics of protein S1 on the 70S ribosome visualized by ensemble cryo-EM.
Article in Methods (San Diego, Calif.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
35 citing papers in PubMed, 45 citations in OpenAlex.
- Structure of the 30S translation initiation complex coupled to paused RNA polymerase and its potential for riboregulation.Nature communications · 2025Article
- In Vivo Ribosome-Amplified MetaBOlism, RAMBO, Effect Observed by Real Time Pulse Chase, RTPC, NMR Spectroscopy.Biochemistry · 2025Article
- Role of Ribosomal Protein bS1 in Orthogonal mRNA Start Codon Selection.Biochemistry · 2025Article
- Molecular basis of mRNA delivery to the bacterial ribosome.Science (New York, N.Y.) · 2024Article
- How Dedicated Ribosomes Translate a Leaderless mRNA.Journal of molecular biology · 2024Article
- Cryo- EM structure of the mycobacterial 70S ribosome in complex with ribosome hibernation promotion factor RafH.Nature communications · 2024Article
- Ribosomal mutations enable a switch between high fitness and high stress resistance inFrontiers in microbiology · 2024Article
- Structural insight into translation initiation of thebioRxiv : the preprint server for biology · 2023Article
- Structural insights into the binding of bS1 to the ribosome.Nucleic acids research · 2023Article
- Precise tuning of bacterial translation initiation by non-equilibrium 5'-UTR unfolding observed in single mRNAs.Nucleic acids research · 2022Article
- Interaction between Phage T4 Protein RIII and Host Ribosomal Protein S1 Inhibits Endoribonuclease RegB Activation.International journal of molecular sciences · 2022Article
- Translation initiation site of mRNA is selected through dynamic interaction with the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Article
- In vitro reconstitution of the Escherichia coli 70S ribosome with a full set of recombinant ribosomal proteins.Journal of biochemistry · 2022Article
- Multiple Antimicrobial Effects of Hybrid Peptides Synthesized Based on the Sequence of Ribosomal S1 Protein fromInternational journal of molecular sciences · 2022Article
- Macromolecular assemblies supporting transcription-translation coupling.Transcription · 2021Review
- 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
- Simplification of Ribosomes in Bacteria with Tiny Genomes.Molecular biology and evolution · 2021Article
- Antimicrobial and Amyloidogenic Activity of Peptides. Can Antimicrobial Peptides Be Used against SARS-CoV-2?International journal of molecular sciences · 2020Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Bacterial ribosomal protein S1 is the largest and highly flexible protein of the 30S subunit, and one of a few core ribosomal proteins for which a complete structure is lacking. S1 is thought to participate in transcription and translation. Best understood is the role of S1 in facilitating translation of mRNAs with structured 5' UTRs. Here, we present cryo-EM analyses of the 70S ribosome that reveal multiple conformations of S1. Based on comparison of several 3D maximum likelihood classification approaches in Frealign, we propose a streamlined strategy for visualizing a highly dynamic component of a large macromolecular assembly that itself exhibits high compositional and conformational heterogeneity. The resulting maps show how S1 docks at the ribosomal protein S2 near the mRNA exit channel. The globular OB-fold domains sample a wide area around the mRNA exit channel and interact with mobile tails of proteins S6 and S18. S1 also interacts with the mRNA entrance channel, where an OB-fold domain can be localized near S3 and S5. Our analyses suggest that S1 cooperates with other ribosomal proteins to form a dynamic mesh near the mRNA exit and entrance channels to modulate the binding, folding and movement of mRNA.
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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.