ArticleNucleic acids research2022
Uncovering translation roadblocks during the development of a synthetic tRNA.
Article in Nucleic acids research, 2022. 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, 14 citations in OpenAlex.
- A comprehensive benchmarking of the AlphaFold3 for predicting biomacromolecules and their interactions.Briefings in bioinformatics · 2025Article
- Comparative analyses ofComputational and structural biotechnology journal · 2024Article
- Overcoming Challenges with Biochemical Studies of Selenocysteine and Selenoproteins.International journal of molecular sciences · 2024Review
- Decomposing bulk signals to reveal hidden information in processive enzyme reactions: A case study in mRNA translation.PLoS computational biology · 2024Article
- tRNA therapeutics for genetic diseases.Nature reviews. Drug discovery · 2024Review
- tRNA shape is an identity element for an archaeal pyrrolysyl-tRNA synthetase from the human gut.Nucleic acids research · 2024Article
- Suppressor tRNAs at the interface of genetic code expansion and medicine.Frontiers in genetics · 2024Review
- Tuning tRNAs for improved translation.Frontiers in genetics · 2024Review
- Recoding UAG to selenocysteine inRNA (New York, N.Y.) · 2023Article
- Dual incorporation of non-canonical amino acids enables production of post-translationally modified selenoproteins.Frontiers in molecular biosciences · 2023Article
- Harnessing selenocysteine to enhance microbial cell factories for hydrogen production.Frontiers in catalysis · 2022Article
Corrections and comments
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Authors and funding
14 authors at 4 institutions in 2 countries.
Funding
Abstract
Ribosomes are remarkable in their malleability to accept diverse aminoacyl-tRNA substrates from both the same organism and other organisms or domains of life. This is a critical feature of the ribosome that allows the use of orthogonal translation systems for genetic code expansion. Optimization of these orthogonal translation systems generally involves focusing on the compatibility of the tRNA, aminoacyl-tRNA synthetase, and a non-canonical amino acid with each other. As we expand the diversity of tRNAs used to include non-canonical structures, the question arises as to the tRNA suitability on the ribosome. Specifically, we investigated the ribosomal translation of allo-tRNAUTu1, a uniquely shaped (9/3) tRNA exploited for site-specific selenocysteine insertion, using single-molecule fluorescence. With this technique we identified ribosomal disassembly occurring from translocation of allo-tRNAUTu1 from the A to the P site. Using cryo-EM to capture the tRNA on the ribosome, we pinpointed a distinct tertiary interaction preventing fluid translocation. Through a single nucleotide mutation, we disrupted this tertiary interaction and relieved the translation roadblock. With the continued diversification of genetic code expansion, our work highlights a targeted approach to optimize translation by distinct tRNAs as they move through the ribosome.
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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.