ArticleNucleic acids research2014
Molecular insights into replication initiation by Qβ replicase using ribosomal protein S1.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 40 citations in OpenAlex.
- A jumbo cyanophage encodes the most comprehensive ribosomal protein set in the known virosphere.The ISME journal · 2026Article
- Reversible acetylation of ribosomal protein S1 serves as a smart switch for Salmonella to rapidly adapt to host stress.Nucleic acids research · 2025Article
- Extraribosomal Functions of Bacterial Ribosomal Proteins-An Update, 2023.International journal of molecular sciences · 2024Review
- Review
- Structural insights into the binding of bS1 to the ribosome.Nucleic acids research · 2023Article
- Hfq protein and GcvB small RNA tailoring ofRNA biology · 2023Article
- Interaction between Phage T4 Protein RIII and Host Ribosomal Protein S1 Inhibits Endoribonuclease RegB Activation.International journal of molecular sciences · 2022Article
- Mechanistic insights into tRNA cleavage by a contact-dependent growth inhibitor protein and translation factors.Nucleic acids research · 2022Article
- Transcription complexes as RNA chaperones.Transcription · 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
- Article
- Allosteric activation of SARS-CoV-2 RdRp by remdesivir triphosphate and other phosphorylated nucleotides.bioRxiv : the preprint server for biology · 2021Article
- Review
- Picornaviruses: A View from 3A.Viruses · 2021Review
- Translation inhibition from a distance: The small RNA SgrS silences a ribosomal protein S1-dependent enhancer.Molecular microbiology · 2020Article
- Structural analysis of 70S ribosomes by cross-linking/mass spectrometry reveals conformational plasticity.Scientific reports · 2020Article
- The Single-Stranded RNA Bacteriophage Qβ Adapts Rapidly to High Temperatures: An Evolution Experiment.Viruses · 2020Article
- Protein unties the pseudoknot: S1-mediated unfolding of RNA higher order structure.Nucleic acids research · 2020Article
- Structural transition of replicable RNAs during in vitro evolution with Qβ replicase.RNA (New York, N.Y.) · 2020Article
- Cell-free expression of RNA encoded genes using MS2 replicase.Nucleic acids research · 2019Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribosomal protein S1, consisting of six contiguous OB-folds, is the largest ribosomal protein and is essential for translation initiation in Escherichia coli. S1 is also one of the three essential host-derived subunits of Qβ replicase, together with EF-Tu and EF-Ts, for Qβ RNA replication in E. coli. We analyzed the crystal structure of Qβ replicase, consisting of the virus-encoded RNA-dependent RNA polymerase (β-subunit), EF-Tu, EF-Ts and the N-terminal half of S1, which is capable of initiating Qβ RNA replication. Structural and biochemical studies revealed that the two N-terminal OB-folds of S1 anchor S1 onto the β-subunit, and the third OB-fold is mobile and protrudes beyond the surface of the β-subunit. The third OB-fold mainly interacts with a specific RNA fragment derived from the internal region of Qβ RNA, and its RNA-binding ability is required for replication initiation of Qβ RNA. Thus, the third mobile OB-fold of S1, which is spatially anchored near the surface of the β-subunit, primarily recruits the Qβ RNA toward the β-subunit, leading to the specific and efficient replication initiation of Qβ RNA, and S1 functions as a replication initiation factor, beyond its established function in protein synthesis.
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