ArticleProceedings of the National Academy of Sciences of the United States of America2018
Atomic mutagenesis of stop codon nucleotides reveals the chemical prerequisites for release factor-mediated peptide release.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 31 citations in OpenAlex.
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- 1-Deazaguanosine-Modified RNA: The Missing Piece for Functional RNA Atomic Mutagenesis.Journal of the American Chemical Society · 2022Article
- Chemical modifications to mRNA nucleobases impact translation elongation and termination.Biophysical chemistry · 2022Review
- A systematic dissection of determinants and consequences of snoRNA-guided pseudouridylation of human mRNA.Nucleic acids research · 2022Article
- Molecular Determinants and Specificity of mRNA with Alternatively-Spliced UPF1 Isoforms, Influenced by an Insertion in the 'Regulatory Loop'.International journal of molecular sciences · 2021Article
- Impact of 3-deazapurine nucleobases on RNA properties.Nucleic acids research · 2021Article
- Investigating the consequences of mRNA modifications on protein synthesis using in vitro translation assays.Methods in enzymology · 2021Article
- Oxidative Modifications of RNA and Its Potential Roles in Biosystem.Frontiers in molecular biosciences · 2021Review
- Termi-Luc: a versatile assay to monitor full-protein release from ribosomes.RNA (New York, N.Y.) · 2020Article
- A molecular-level perspective on the frequency, distribution, and consequences of messenger RNA modifications.Wiley interdisciplinary reviews. RNA · 2020Review
- Strategies for in vitro engineering of the translation machinery.Nucleic acids research · 2020Review
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- Translation of non-standard codon nucleotides reveals minimal requirements for codon-anticodon interactions.Nature communications · 2018Article
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Authors and funding
12 authors at 4 institutions in 3 countries.
Funding
Abstract
Termination of protein synthesis is triggered by the recognition of a stop codon at the ribosomal A site and is mediated by class I release factors (RFs). Whereas in bacteria, RF1 and RF2 promote termination at UAA/UAG and UAA/UGA stop codons, respectively, eukaryotes only depend on one RF (eRF1) to initiate peptide release at all three stop codons. Based on several structural as well as biochemical studies, interactions between mRNA, tRNA, and rRNA have been proposed to be required for stop codon recognition. In this study, the influence of these interactions was investigated by using chemically modified stop codons. Single functional groups within stop codon nucleotides were substituted to weaken or completely eliminate specific interactions between the respective mRNA and RFs. Our findings provide detailed insight into the recognition mode of bacterial and eukaryotic RFs, thereby revealing the chemical groups of nucleotides that define the identity of stop codons and provide the means to discriminate against noncognate stop codons or UGG sense codons.
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