ArticleNucleic acids research2015
Structural basis for RNA-genome recognition during bacteriophage Qβ replication.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 22 citations in OpenAlex.
- 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
- Article
- Protein unties the pseudoknot: S1-mediated unfolding of RNA higher order structure.Nucleic acids research · 2020Article
- Expansion of known ssRNA phage genomes: From tens to over a thousand.Science advances · 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
- Article
- In situ structures of rotavirus polymerase in action and mechanism of mRNA transcription and release.Nature communications · 2019Article
- The number of domains in the ribosomal protein S1 as a hallmark of the phylogenetic grouping of bacteria.PloS one · 2019Article
- RNA Phage Biology in a Metagenomic Era.Viruses · 2018Review
- Review
- Structures of Qβ virions, virus-like particles, and the Qβ-MurA complex reveal internal coat proteins and the mechanism of host lysis.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Upon infection of Escherichia coli by bacteriophage Qβ, the virus-encoded β-subunit recruits host translation elongation factors EF-Tu and EF-Ts and ribosomal protein S1 to form the Qβ replicase holoenzyme complex, which is responsible for amplifying the Qβ (+)-RNA genome. Here, we use X-ray crystallography, NMR spectroscopy, as well as sequence conservation, surface electrostatic potential and mutational analyses to decipher the roles of the β-subunit and the first two oligonucleotide-oligosaccharide-binding domains of S1 (OB1-2) in the recognition of Qβ (+)-RNA by the Qβ replicase complex. We show how three basic residues of the β subunit form a patch located adjacent to the OB2 domain, and use NMR spectroscopy to demonstrate for the first time that OB2 is able to interact with RNA. Neutralization of the basic residues by mutagenesis results in a loss of both the phage infectivity in vivo and the ability of Qβ replicase to amplify the genomic RNA in vitro. In contrast, replication of smaller replicable RNAs is not affected. Taken together, our data suggest that the β-subunit and protein S1 cooperatively bind the (+)-stranded Qβ genome during replication initiation and provide a foundation for understanding template discrimination during replication initiation.
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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.