ArticleProceedings of the National Academy of Sciences of the United States of America2008
RNA-assisted catalysis in a protein enzyme: The 2'-hydroxyl of tRNA(Thr) A76 promotes aminoacylation by threonyl-tRNA synthetase.
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 28 papers.
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Who cites it
28 citing papers in PubMed, 56 citations in OpenAlex.
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- Negative catalysis by the editing domain of class I aminoacyl-tRNA synthetases.Nucleic acids research · 2022Article
- Possible Ancestral Functions of the Genetic and RNA Operational Precodes and the Origin of the Genetic System.Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life · 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
- RNA Structural Dynamics As Captured by Molecular Simulations: A Comprehensive Overview.Chemical reviews · 2018Review
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- Characterization of aminoacyl-tRNA synthetase stability and substrate interaction by differential scanning fluorimetry.Methods (San Diego, Calif.) · 2017Review
- Aminoacyl-tRNA synthetase dependent angiogenesis revealed by a bioengineered macrolide inhibitor.Scientific reports · 2015Article
- MD Simulations of tRNA and Aminoacyl-tRNA Synthetases: Dynamics, Folding, Binding, and Allostery.International journal of molecular sciences · 2015Review
- Specificity and catalysis hardwired at the RNA-protein interface in a translational proofreading enzyme.Nature communications · 2015Article
- The juxtaposition of ribose hydroxyl groups: the root of biological catalysis and the RNA world?Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life · 2015Article
- The tRNA A76 Hydroxyl Groups Control Partitioning of the tRNA-dependent Pre- and Post-transfer Editing Pathways in Class I tRNA Synthetase.The Journal of biological chemistry · 2015Article
- Multi-scale computational enzymology: enhancing our understanding of enzymatic catalysis.International journal of molecular sciences · 2013Review
- Aminoacyl-tRNA substrate and enzyme backbone atoms contribute to translational quality control by YbaK.The journal of physical chemistry. B · 2013Article
- Kinetic partitioning between synthetic and editing pathways in class I aminoacyl-tRNA synthetases occurs at both pre-transfer and post-transfer hydrolytic steps.The Journal of biological chemistry · 2012Article
- Substrate and enzyme functional groups contribute to translational quality control by bacterial prolyl-tRNA synthetase.The journal of physical chemistry. B · 2012Article
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
Aminoacyl-tRNA synthetases (aaRSs) join amino acids to 1 of 2 terminal hydroxyl groups of their cognate tRNAs, thereby contributing to the overall fidelity of protein synthesis. In class II histidyl-tRNA synthetase (HisRS) the nonbridging S(p)-oxygen of the adenylate is a potential general base for aminoacyl transfer. To test for conservation of this mechanism in other aaRSs and the role of terminal hydroxyls of tRNA in aminoacyl transfer, we investigated the class II Escherichia coli threonyl-tRNA synthetase (ThrRS). As with other class II aaRSs, the rate-determining step for ThrRS is amino acid activation. In ThrRS, however, the 2'-OH of A76 of tRNA(Thr) and a conserved active-site histidine (His-309) collaborate to catalyze aminoacyl transfer by a mechanism distinct from HisRS. Conserved residues in the ThrRS active site were replaced with alanine, and then the resulting mutant proteins were analyzed by steady-state and rapid kinetics. Nearly all mutants preferentially affected the amino acid activation step, with only a modest effect on aminoacyl transfer. By contrast, H309A ThrRS decreased transfer 242-fold and imposed a kinetic block to CCA accommodation. His-309 hydrogen bonds to the 2'-OH of A76, and substitution of the latter by hydrogen or fluorine decreased aminoacyl transfer by 763- and 94-fold, respectively. The proton relay mechanism suggested by these data to promote aminoacylation is reminiscent of the NAD(+)-dependent mechanisms of alcohol dehydrogenases and sirtuins and the RNA-mediated catalysis of the ribosomal peptidyl transferase center.
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