ArticleNucleic acids research2015
The ATP-mediated formation of the YgjD-YeaZ-YjeE complex is required for the biosynthesis of tRNA t6A in Escherichia coli.
Article in Nucleic acids research, 2015. 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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Who cites it
31 citing papers in PubMed.
- Anticodon loop remodeling and D-stem shape drive the specific recognition of ANN-decoding tRNAs for t6A modification.Nucleic acids research · 2026Article
- Catalytic and regulatory basis of tRNA tNature communications · 2026Article
- The Impacts of Essential Gcp/TsaD Protein on Cell Morphology, Virulence Expression, and Antibiotic Susceptibility inMicroorganisms · 2025Article
- Structures of KEOPS bound to tRNA reveal functional roles of the kinase Bud32.Nature communications · 2024Article
- Molecular basis of A. thaliana KEOPS complex in biosynthesizing tRNA t6A.Nucleic acids research · 2024Article
- New Insights into the Biological Functions of Essential TsaB/YeaZ Protein inAntibiotics (Basel, Switzerland) · 2024Article
- Structure-function analysis of an ancient TsaD-TsaC-SUA5-TcdA modular enzyme reveals a prototype of tRNA t6A and ct6A synthetases.Nucleic acids research · 2023Article
- Conservation and Diversification of tRNA tInternational journal of molecular sciences · 2022Review
- Reductions in bacterial viability stimulate the production of Extra-intestinal Pathogenic Escherichia coli (ExPEC) cytoplasm-carrying Extracellular Vesicles (EVs).PLoS pathogens · 2022Article
- Commonality and diversity in tRNA substrate recognition in t6A biogenesis by eukaryotic KEOPSs.Nucleic acids research · 2022Article
- The structural and functional workings of KEOPS.Nucleic acids research · 2021Review
- Predictive approaches to guide the expression of recombinant vaccine targets in Escherichia coli: a case study presentation utilising Absynth Biologics Ltd. proprietary Clostridium difficile vaccine antigens.Applied microbiology and biotechnology · 2021Article
- Structure of a reaction intermediate mimic in t6A biosynthesis bound in the active site of the TsaBD heterodimer from Escherichia coli.Nucleic acids research · 2021Article
- Metal utilization in genome-reduced bacteria: Do human mycoplasmas rely on iron?Computational and structural biotechnology journal · 2021Review
- UbK is Involved in the Resistance of Bacillus Subtilis to Oxidative Stress.Current microbiology · 2020Article
- Specificity in the biosynthesis of the universal tRNA nucleosideRNA (New York, N.Y.) · 2020Article
- Molecular basis for t6A modification in human mitochondria.Nucleic acids research · 2020Article
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- Glucose-Mediated Protein Arginine Phosphorylation/Dephosphorylation RegulatesFrontiers in microbiology · 2020Article
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5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The essential and universal N(6)-threonylcarbamoyladenosine (t(6)A) modification at position 37 of ANN-decoding tRNAs plays a pivotal role in translational fidelity through enhancement of the cognate codon recognition and stabilization of the codon-anticodon interaction. In Escherichia coli, the YgjD (TsaD), YeaZ (TsaB), YjeE (TsaE) and YrdC (TsaC) proteins are necessary and sufficient for the in vitro biosynthesis of t(6)A, using tRNA, ATP, L-threonine and bicarbonate as substrates. YrdC synthesizes the short-lived L-threonylcarbamoyladenylate (TCA), and YgjD, YeaZ and YjeE cooperate to transfer the L-threonylcarbamoyl-moiety from TCA onto adenosine at position 37 of substrate tRNA. We determined the crystal structure of the heterodimer YgjD-YeaZ at 2.3 Å, revealing the presence of an unexpected molecule of ADP bound at an atypical site situated at the YgjD-YeaZ interface. We further showed that the ATPase activity of YjeE is strongly activated by the YgjD-YeaZ heterodimer. We established by binding experiments and SAXS data analysis that YgjD-YeaZ and YjeE form a compact ternary complex only in presence of ATP. The formation of the ternary YgjD-YeaZ-YjeE complex is required for the in vitro biosynthesis of t(6)A but not its ATPase activity.
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