ArticleThe Journal of biological chemistry2022
mRNA and tRNA modification states influence ribosome speed and frame maintenance during poly(lysine) peptide synthesis.
Article in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Review
- Engineered Coiled-Coils Convert Cholera Toxin B-Pentamers into Programmable Membrane Fusogens.ACS nano · 2026Article
- Defining the high-translational readthrough stop codon context.PLoS genetics · 2025Article
- Anticodon stem-loop tRNA modifications influence codon decoding and frame maintenance during translation.Seminars in cell & developmental biology · 2024Review
- Impact of the chemical modification of tRNAs anticodon loop on the variability and evolution of codon usage in proteobacteria.Frontiers in microbiology · 2024Article
- Chemical modifications to mRNA nucleobases impact translation elongation and termination.Biophysical chemistry · 2022Review
- Variance in translational fidelity of different bacterial species is affected by pseudouridines in the tRNA anticodon stem-loop.RNA biology · 2022Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Ribosome speed is dictated by multiple factors including substrate availability, cellular conditions, and product (peptide) formation. Translation slows during the synthesis of cationic peptide sequences, potentially influencing the expression of thousands of proteins. Available evidence suggests that ionic interactions between positively charged nascent peptides and the negatively charged ribosome exit tunnel impede translation. However, this hypothesis was difficult to test directly because of inability to decouple the contributions of amino acid charge from mRNA sequence and tRNA identity/abundance in cells. Furthermore, it is unclear if other components of the translation system central to ribosome function (e.g., RNA modification) influence the speed and accuracy of positively charged peptide synthesis. In this study, we used a fully reconstituted Escherichia coli translation system to evaluate the effects of peptide charge, mRNA sequence, and RNA modification status on the translation of lysine-rich peptides. Comparison of translation reactions on poly(lysine)-encoding mRNAs conducted with either Lys-tRNA
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