ArticleProceedings of the National Academy of Sciences of the United States of America2008
Crystallographic snapshots of eukaryotic dimethylallyltransferase acting on tRNA: insight into tRNA recognition and reaction mechanism.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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30 citing papers in PubMed, 54 citations in OpenAlex.
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- The life and times of a tRNA.RNA (New York, N.Y.) · 2023Review
- Modopathies Caused by Mutations in Genes Encoding for Mitochondrial RNA Modifying Enzymes: Molecular Mechanisms and Yeast Disease Models.International journal of molecular sciences · 2023Review
- Evolutionary Diversity of Dus2 Enzymes Reveals Novel Structural and Functional Features among Members of the RNA Dihydrouridine Synthases Family.Biomolecules · 2022Article
- The Effect of tRNAInternational journal of molecular sciences · 2021Article
- Biochemical and Structural Aspects of Cytokinin Biosynthesis and Degradation in Bacteria.Microorganisms · 2021Review
- Structural, biochemical and functional analyses of tRNA-monooxygenase enzyme MiaE from Pseudomonas putida provide insights into tRNA/MiaE interaction.Nucleic acids research · 2020Article
- Targeting mitochondrial and cytosolic substrates of TRIT1 isopentenyltransferase: Specificity determinants and tRNA-i6A37 profiles.PLoS genetics · 2020Article
- Occurrence and biosynthesis of cytokinins in poplar.Planta · 2019Article
- Molecular basis of tRNA recognition by the Elongator complex.Science advances · 2019Article
- Crystal structure of the Lin28-interacting module of human terminal uridylyltransferase that regulates let-7 expression.Nature communications · 2019Article
- The modified base isopentenyladenosine and its derivatives in tRNA.RNA biology · 2017Review
- Aggregation of Mod5 is affected by tRNA binding with implications for tRNA gene-mediated silencing.FEBS letters · 2017Article
- Violation of DNA neighbor exclusion principle in RNA recognition.Chemical science · 2016Article
- Cytokinin Production by the Rice Blast Fungus Is a Pivotal Requirement for Full Virulence.PLoS pathogens · 2016Article
- Review
- Defective i6A37 modification of mitochondrial and cytosolic tRNAs results from pathogenic mutations in TRIT1 and its substrate tRNA.PLoS genetics · 2014Article
- Structural characterization of interactions between the double-stranded RNA-binding zinc finger protein JAZ and nucleic acids.Biochemistry · 2014Article
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2 authors at 1 institution in 1 country.
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Abstract
Hypermodifications near the anticodon of tRNA are fundamental for the efficiency and fidelity of protein synthesis. Dimethylallyltransferase (DMATase) catalyzes transfer of a dimethylallyl moiety from dimethylallyl pyrophosphate to N6 of A37 in certain tRNAs. Here we present the crystal structures of Saccharomyces cerevisiae DMATase-tRNA(Cys) complex in four distinct forms, which provide snapshots of the RNA modification reaction catalyzed by DMATase. The structures reveal that the enzyme recognizes the tRNA substrate through indirect sequence readout. The targeted nucleotide A37 flips out from the anticodon loop of tRNA and flips into a channel in DMATase, where it meets its reaction partner di methylallyl pyrophosphate, which enters the channel from the opposite end. Structural changes accompanying the transfer reaction taking place in the crystal result in disengagement of DMATase-tRNA interaction near the reaction center. In addition, structural comparison of DMATase in the complex with unliganded bacterial DMATase provides a molecular basis of ordered substrate binding by DMATase.
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