ArticleNucleic acids research2018
Unveiling structural and functional divergences of bacterial tRNA dihydrouridine synthases: perspectives on the evolution scenario.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 citing papers in PubMed, 44 citations in OpenAlex.
- Comprehensive post-transcriptional modification profiles in individual Staphylococcus aureus tRNA species.Nucleic acids research · 2026Article
- Integrated multi-omics analysis of fluoroquinolone tolerance mechanisms induced by enrofloxacin in Pasteurella multocida.BMC microbiology · 2026Article
- Exploring the genetic landscape of ciprofloxacin-induced DNA supercompaction in Escherichia coli.Nucleic acids research · 2026Article
- Contribution of three tRNA modification enzymes toInfection and immunity · 2026Article
- The tRNA dihydrouridine synthase DusA has a distinct mechanism in optimizing tRNAs for translation.Nucleic acids research · 2026Article
- Beyond RNA modification: a novel role for tRNA modifying enzyme in oxidative stress response and metabolism.Nucleic acids research · 2025Article
- tRNA Modification Landscapes in Streptococci: Shared Losses and Clade-Specific Adaptations.bioRxiv : the preprint server for biology · 2025Article
- Differential redox sensitivity of tRNA dihydrouridylation.Nucleic acids research · 2024Article
- DORQ-seq: high-throughput quantification of femtomol tRNA pools by combination of cDNA hybridization and Deep sequencing.Nucleic acids research · 2024Article
- Human DUS1L catalyzes dihydrouridine modification at tRNA positions 16/17, and DUS1L overexpression perturbs translation.Communications biology · 2024Article
- Exploring a unique class of flavoenzymes: Identification and biochemical characterization of ribosomal RNA dihydrouridine synthase.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Functional redundancy in tRNA dihydrouridylation.Nucleic acids research · 2024Article
- Mapping the tRNA modification landscape ofFrontiers in microbiology · 2024Article
- Escherichia coli tRNA (Gm18) methyltransferase (TrmH) requires the correct localization of its methylation site (G18) in the D-loop for efficient methylation.Journal of biochemistry · 2023Article
- Integrative Approach to Probe Alternative Redox Mechanisms in RNA Modifications.Accounts of chemical research · 2023Article
- Review
- Evolutionary Diversity of Dus2 Enzymes Reveals Novel Structural and Functional Features among Members of the RNA Dihydrouridine Synthases Family.Biomolecules · 2022Article
- Nonessential tRNA and rRNA modifications impact the bacterial response to sub-MIC antibiotic stress.microLife · 2022Article
- The Dihydrouridine landscape from tRNA to mRNA: a perspective on synthesis, structural impact and function.RNA biology · 2022Review
- Article
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Post-transcriptional base modifications are important to the maturation process of transfer RNAs (tRNAs). Certain modifications are abundant and present at several positions in tRNA as for example the dihydrouridine, a modified base found in the three domains of life. Even though the function of dihydrourine is not well understood, its high content in tRNAs from psychrophilic bacteria or cancer cells obviously emphasizes a central role in cell adaptation. The reduction of uridine to dihydrouridine is catalyzed by a large family of flavoenzymes named dihydrouridine synthases (Dus). Prokaryotes have three Dus (A, B and C) wherein DusB is considered as an ancestral protein from which the two others derived via gene duplications. Here, we unequivocally established the complete substrate specificities of the three Escherichia coli Dus and solved the crystal structure of DusB, enabling for the first time an exhaustive structural comparison between these bacterial flavoenzymes. Based on our results, we propose an evolutionary scenario explaining how substrate specificities has been diversified from a single structural fold.
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