ArticleNucleic acids research2026
The tRNA dihydrouridine synthase DusA has a distinct mechanism in optimizing tRNAs for translation.
Article in Nucleic acids research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Contribution of three tRNA modification enzymes toInfection and immunity · 2026Article
- Beyond RNA modification: a novel role for tRNA modifying enzyme in oxidative stress response and metabolism.Nucleic acids research · 2025Article
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Authors and funding
6 authors.
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Abstract
Dihydrouridine (D) is one of the most highly conserved RNA modifications across all domains of life. D20 within the tRNA D loop is particularly conserved and is formed by DusA in Escherichia coli. However, the mechanisms and cellular functions of DusA and D20 remain poorly understood. Here, we characterize DusA's role in tRNA binding, cofactor oxidation, and modification activity, along with its impact on tRNA maturation and translation. We find that DusA binds tRNA via a two-step mechanism involving a local structural rearrangement and exhibits a higher affinity for previously modified tRNA compared to unmodified tRNA. Unlike the T arm modifying enzymes TrmA and TruB, DusA does not broadly increase cellular aminoacylation for all tRNAs but enhances the charging of specific tRNA species. Despite limited alterations in overall tRNA charging and abundance in cells lacking DusA, DusA selectively improves translation at several specific codons, potentially indicating a direct contribution for dihydrouridine to the function of certain tRNAs on the ribosome. In conclusion, our findings suggest DusA acts nonredundantly with and complementary to TrmA and TruB in fine-tuning protein synthesis.
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