ArticleNucleic acids research2021
Twice exploration of tRNA +1 frameshifting in an elongation cycle of protein synthesis.
Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- EF-G Mutations Reveal Correlation between Power Stroke and Translocation Fidelity in Protein Synthesis.bioRxiv : the preprint server for biology · 2025Article
- Connecting tRNA Charging and Decoding through the Axis of Nucleotide Modifications at Position 37.Journal of molecular biology · 2025Review
- An RNA modification prevents extended codon-anticodon interactions from facilitating +1 frameshifting.Nature communications · 2025Article
- Genome-wide profiling of tRNA modifications by Induro-tRNAseq reveals coordinated changes.Nature communications · 2025Article
- Engineering tRNAs for the Ribosomal Translation of Non-proteinogenic Monomers.Chemical reviews · 2024Review
- Ribosomal frameshifting at normal codon repeats recodes functional chimeric proteins in human.Nucleic acids research · 2024Article
- A tRNA modification pattern that facilitates interpretation of the genetic code.Frontiers in microbiology · 2024Article
- Synthesis of Stably Charged Arg-tRNAMethods in molecular biology (Clifton, N.J.) · 2023Article
- tRNA methylation resolves codon usage bias at the limit of cell viability.Cell reports · 2022Article
- Genome Expansion by tRNA +1 Frameshifting at Quadruplet Codons.Journal of molecular biology · 2022Review
- Thinking Outside the Frame: Impacting Genomes Capacity by Programmed Ribosomal Frameshifting.Frontiers in molecular biosciences · 2022Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Inducing tRNA +1 frameshifting to read a quadruplet codon has the potential to incorporate a non-natural amino acid into the polypeptide chain. While this strategy is being considered for genome expansion in biotechnology and bioengineering endeavors, a major limitation is a lack of understanding of where the shift occurs in an elongation cycle of protein synthesis. Here, we use the high-efficiency +1-frameshifting SufB2 tRNA, containing an extra nucleotide in the anticodon loop, to address this question. Physical and kinetic measurements of the ribosome reading frame of SufB2 identify twice exploration of +1 frameshifting in one elongation cycle, with the major fraction making the shift during translocation from the aminoacyl-tRNA binding (A) site to the peptidyl-tRNA binding (P) site and the remaining fraction making the shift within the P site upon occupancy of the A site in the +1-frame. We demonstrate that the twice exploration of +1 frameshifting occurs during active protein synthesis and that each exploration is consistent with ribosomal conformational dynamics that permits changes of the reading frame. This work indicates that the ribosome itself is a determinant of changes of the reading frame and reveals a mechanistic parallel of +1 frameshifting with -1 frameshifting.
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Registered trials
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.