ArticleNature communications2015
Specificity and catalysis hardwired at the RNA-protein interface in a translational proofreading enzyme.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
17 citing papers in PubMed.
- Mechanistic and evolutionary insights into a family of aminoacyl-tRNA deacylases that protects against canavanine toxicity.Nucleic acids research · 2025Article
- Mammalian Tolerance to Amino Acid Heterochirality.Chembiochem : a European journal of chemical biology · 2025Review
- When Paul Berg meets Donald Crothers: an achiral connection through protein biosynthesis.Nucleic acids research · 2024Article
- CAT-Site: Predicting Protein Binding Sites Using a Convolutional Neural Network.Pharmaceutics · 2022Article
- Negative catalysis by the editing domain of class I aminoacyl-tRNA synthetases.Nucleic acids research · 2022Article
- Indirect Routes to Aminoacyl-tRNA: The Diversity of Prokaryotic Cysteine Encoding Systems.Frontiers in genetics · 2021Article
- A revised mechanism for (p)ppGpp synthesis by Rel proteins: The critical role of the 2'-OH of GTP.The Journal of biological chemistry · 2020Article
- Chiral checkpoints during protein biosynthesis.The Journal of biological chemistry · 2019Review
- Small Molecule Catalysts with Therapeutic Potential.Molecules (Basel, Switzerland) · 2018Review
- A chiral selectivity relaxed paralog of DTD for proofreading tRNA mischarging in Animalia.Nature communications · 2018Article
- Article
- Discovery and Investigation of Natural Editing Function against Artificial Amino Acids in Protein Translation.ACS central science · 2017Article
- An RNA Binding Peptide Consisting of Four Types of Amino Acid by in Vitro Selection Using cDNA Display.ACS omega · 2016Article
- Elongation Factor Tu Prevents Misediting of Gly-tRNA(Gly) Caused by the Design Behind the Chiral Proofreading Site of D-Aminoacyl-tRNA Deacylase.PLoS biology · 2016Article
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
- Recent Updates on DTD (D-Tyr-tRNA(Tyr) Deacylase): An Enzyme Essential for Fidelity and Quality of Protein Synthesis.Frontiers in cell and developmental biology · 2016Review
- Evolutionary Limitation and Opportunities for Developing tRNA Synthetase Inhibitors with 5-Binding-Mode Classification.Life (Basel, Switzerland) · 2015Review
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proofreading modules of aminoacyl-tRNA synthetases are responsible for enforcing a high fidelity during translation of the genetic code. They use strategically positioned side chains for specifically targeting incorrect aminoacyl-tRNAs. Here, we show that a unique proofreading module possessing a D-aminoacyl-tRNA deacylase fold does not use side chains for imparting specificity or for catalysis, the two hallmark activities of enzymes. We show, using three distinct archaea, that a side-chain-stripped recognition site is fully capable of solving a subtle discrimination problem. While biochemical probing establishes that RNA plays the catalytic role, mechanistic insights from multiple high-resolution snapshots reveal that differential remodelling of the catalytic core at the RNA-peptide interface provides the determinants for correct proofreading activity. The functional crosstalk between RNA and protein elucidated here suggests how primordial enzyme functions could have emerged on RNA-peptide scaffolds before recruitment of specific side chains.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.