ReviewBiochemistry2008
DNA polymerases and aminoacyl-tRNA synthetases: shared mechanisms for ensuring the fidelity of gene expression.
Review in Biochemistry, 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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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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
28 citing papers in PubMed.
- Translation in Mitochondrial Ribosomes.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Impact of alanyl-tRNA synthetase editing deficiency in yeast.Nucleic acids research · 2021Article
- Metabolic stress promotes stop-codon readthrough and phenotypic heterogeneity.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Editing Domain Motions Preorganize the Synthetic Active Site of Prolyl-tRNA Synthetase.ACS catalysis · 2020Article
- The nature of the purine at position 34 in tRNAs of 4-codon boxes is correlated with nucleotides at positions 32 and 38 to maintain decoding fidelity.Nucleic acids research · 2020Article
- Optimal translational fidelity is critical for Salmonella virulence and host interactions.Nucleic acids research · 2019Article
- Genomic characterization of three novel Basilisk-like phages infecting Bacillus anthracis.BMC genomics · 2018Article
- Review
- rAMPing Up Stress Signaling: Protein AMPylation in Metazoans.Trends in cell biology · 2017Review
- Global analysis of translation termination in E. coli.PLoS genetics · 2017Article
- Reduced Protein Synthesis Fidelity Inhibits Flagellar Biosynthesis and Motility.Scientific reports · 2016Article
- The ribosome prohibits the G•U wobble geometry at the first position of the codon-anticodon helix.Nucleic acids research · 2016Article
- Structures of two bacterial resistance factors mediating tRNA-dependent aminoacylation of phosphatidylglycerol with lysine or alanine.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- MD Simulations of tRNA and Aminoacyl-tRNA Synthetases: Dynamics, Folding, Binding, and Allostery.International journal of molecular sciences · 2015Review
- Proteomic analysis of Apis cerana and Apis mellifera larvae fed with heterospecific royal jelly and by CSBV challenge.PloS one · 2014Article
- Recognition of Watson-Crick base pairs: constraints and limits due to geometric selection and tautomerism.F1000prime reports · 2014Review
- Multi-scale computational enzymology: enhancing our understanding of enzymatic catalysis.International journal of molecular sciences · 2013Review
- Reorganization of an intersubunit bridge induced by disparate 16S ribosomal ambiguity mutations mimics an EF-Tu-bound state.Proceedings of the National Academy of Sciences of the United States of America · 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
- The α-amino group of the threonine substrate as the general base during tRNA aminoacylation: a new version of substrate-assisted catalysis predicted by hybrid DFT.The journal of physical chemistry. A · 2011Article
Corrections and comments
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Authors and funding
1 author.
Funding
Abstract
DNA polymerases and aminoacyl-tRNA synthetases (ARSs) represent large enzyme families with critical roles in the transformation of genetic information from DNA to RNA to protein. DNA polymerases carry out replication and collaborate in the repair of the genome, while ARSs provide aminoacylated tRNA precursors for protein synthesis. Enzymes of both families face the common challenge of selecting their cognate small molecule substrates from a pool of chemically related molecules, achieving high levels of discrimination with the assistance of proofreading mechanisms. Here, the fidelity preservation mechanisms in these two important systems are reviewed and similar features highlighted. Among the noteworthy features common to both DNA polymerases and ARSs are the use of multidomain architectures that segregate synthetic and proofreading functions into discrete domains; the use of induced fit to enhance binding selectivity; the imposition of fidelity at the level of chemistry; and the use of postchemistry error correction mechanisms to hydrolyze incorrect products in a discrete editing domain. These latter mechanisms further share the common property that error correction involves the translocation of misincorporated products from the synthetic to the editing site and that the accuracy of the process may be influenced by the rates of translocation in either direction. Fidelity control in both families can thus be said to rely on multiple elementary steps, each with its contribution to overall fidelity. The summed contribution of these kinetic checkpoints provides the high observed overall accuracy of DNA replication and aminoacylation.
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Registered trials
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.