ArticleRNA (New York, N.Y.)2011
Pre-steady-state kinetic analysis of the three Escherichia coli pseudouridine synthases TruB, TruA, and RluA reveals uniformly slow catalysis.
Article in RNA (New York, N.Y.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 34 citations in OpenAlex.
- Reduced sensitivity to RNA structural differences distinguishes eukaryotic Pus4 from bacterial TruB.RNA (New York, N.Y.) · 2026Article
- The tRNA dihydrouridine synthase DusA has a distinct mechanism in optimizing tRNAs for translation.Nucleic acids research · 2026Article
- Review
- Different modification pathways for m1A58 incorporation in yeast elongator and initiator tRNAs.Nucleic acids research · 2023Article
- Pseudouridine synthase 7 is an opportunistic enzyme that binds and modifies substrates with diverse sequences and structures.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Synergistic interaction network between the snR30 RNP, Utp23, and ribosomal RNA during ribosome synthesis.RNA biology · 2022Article
- Adaptor Molecules Epitranscriptome Reprograms Bacterial Pathogenicity.International journal of molecular sciences · 2021Review
- The tRNA pseudouridine synthase TruB1 regulates the maturation of let-7 miRNA.The EMBO journal · 2020Article
- tRNA elbow modifications affect the tRNA pseudouridine synthase TruB and the methyltransferase TrmA.RNA (New York, N.Y.) · 2020Article
- The methyltransferase TrmA facilitates tRNA folding through interaction with its RNA-binding domain.Nucleic acids research · 2020Article
- Efficient RNA pseudouridylation by eukaryotic H/ACA ribonucleoproteins requires high affinity binding and correct positioning of guide RNA.Nucleic acids research · 2018Article
- RNA modification enzyme TruB is a tRNA chaperone.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The Pseudouridine Synthases Proceed through a Glycal Intermediate.Journal of the American Chemical Society · 2016Article
- Dye label interference with RNA modification reveals 5-fluorouridine as non-covalent inhibitor.Nucleic acids research · 2014Article
- An arginine-aspartate network in the active site of bacterial TruB is critical for catalyzing pseudouridine formation.Nucleic acids research · 2014Article
- Pseudouridine: still mysterious, but never a fake (uridine)!RNA biology · 2014Review
- RNase-L deficiency exacerbates experimental colitis and colitis-associated cancer.Inflammatory bowel diseases · 2013Article
- Kinetic and thermodynamic characterization of the reaction pathway of box H/ACA RNA-guided pseudouridine formation.Nucleic acids research · 2012Article
- Archaeal proteins Nop10 and Gar1 increase the catalytic activity of Cbf5 in pseudouridylating tRNA.Scientific reports · 2012Article
- Review
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4 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Pseudouridine synthases catalyze formation of the most abundant modification of functional RNAs by site-specifically isomerizing uridines to pseudouridines. While the structure and substrate specificity of these enzymes have been studied in detail, the kinetic and the catalytic mechanism of pseudouridine synthases remain unknown. Here, the first pre-steady-state kinetic analysis of three Escherichia coli pseudouridine synthases is presented. A novel stopped-flow absorbance assay revealed that substrate tRNA binding by TruB takes place in two steps with an overall rate of 6 sec(-1). In order to observe catalysis of pseudouridine formation directly, the traditional tritium release assay was adapted for the quench-flow technique, allowing, for the first time, observation of a single round of pseudouridine formation. Thereby, the single-round rate constant of pseudouridylation (k(Ψ)) by TruB was determined to be 0.5 sec(-1). This rate constant is similar to the k(cat) obtained under multiple-turnover conditions in steady-state experiments, indicating that catalysis is the rate-limiting step for TruB. In order to investigate if pseudouridine synthases are characterized by slow catalysis in general, the rapid kinetic quench-flow analysis was also performed with two other E. coli enzymes, RluA and TruA, which displayed rate constants of pseudouridine formation of 0.7 and 0.35 sec(-1), respectively. Hence, uniformly slow catalysis might be a general feature of pseudouridine synthases that share a conserved catalytic domain and supposedly use the same catalytic mechanism.
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