ArticleNucleic acids research2007
Structural basis for recognition of cognate tRNA by tyrosyl-tRNA synthetase from three kingdoms.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
34 citing papers in PubMed.
- The highly conserved intron of tyrosine tRNA is critical forProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Yeast models for Charcot-Marie-Tooth disease-causing aminoacyl-tRNA synthetase alleles reveal the cellular basis of disease.IUBMB life · 2025Review
- BeyondChemical reviews · 2025Review
- Structural insights into dynamics of the BMV TLS aminoacylation.Nature communications · 2025Article
- Engineering tRNAs for the Ribosomal Translation of Non-proteinogenic Monomers.Chemical reviews · 2024Review
- Diversity and modularity of tyrosine-accepting tRNA-like structures.RNA (New York, N.Y.) · 2024Article
- tRNA therapeutics for genetic diseases.Nature reviews. Drug discovery · 2024Review
- Rewiring of Aminoacyl-tRNA Synthetase Localization and Interactions in Plants With Extensive Mitochondrial tRNA Gene Loss.Molecular biology and evolution · 2023Article
- Site-specific dual encoding and labeling of proteins via genetic code expansion.Cell chemical biology · 2023Review
- The tRNA identity landscape for aminoacylation and beyond.Nucleic acids research · 2023Review
- A missense, loss-of-functionCold Spring Harbor molecular case studies · 2022Article
- The promise of cryo-EM to explore RNA structural dynamics.Journal of molecular biology · 2022Review
- Genetic Code Engineering by Natural and Unnatural Base Pair Systems for the Site-Specific Incorporation of Non-Standard Amino Acids Into Proteins.Frontiers in molecular biosciences · 2022Review
- A viral RNA hijacks host machinery using dynamic conformational changes of a tRNA-like structure.Science (New York, N.Y.) · 2021Article
- Mammalian NSUN2 introduces 5-methylcytidines into mitochondrial tRNAs.Nucleic acids research · 2019Article
- Multiple Click-Selective tRNA Synthetases Expand Mammalian Cell-Specific Proteomics.Journal of the American Chemical Society · 2018Article
- Article
- Identifying the ligated amino acid of archaeal tRNAs based on positions outside the anticodon.RNA (New York, N.Y.) · 2016Article
- Identification and characterization of mutations conferring resistance to D-amino acids in Bacillus subtilis.Journal of bacteriology · 2015Article
- Ancestral Reconstruction of a Pre-LUCA Aminoacyl-tRNA Synthetase Ancestor Supports the Late Addition of Trp to the Genetic Code.Journal of molecular evolution · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The specific aminoacylation of tRNA by tyrosyl-tRNA synthetases (TyrRSs) relies on the identity determinants in the cognate tRNA(Tyr)s. We have determined the crystal structure of Saccharomyces cerevisiae TyrRS (SceTyrRS) complexed with a Tyr-AMP analog and the native tRNA(Tyr)(GPsiA). Structural information for TyrRS-tRNA(Tyr) complexes is now full-line for three kingdoms. Because the archaeal/eukaryotic TyrRSs-tRNA(Tyr)s pairs do not cross-react with their bacterial counterparts, the recognition modes of the identity determinants by the archaeal/eukaryotic TyrRSs were expected to be similar to each other but different from that by the bacterial TyrRSs. Interestingly, however, the tRNA(Tyr) recognition modes of SceTyrRS have both similarities and differences compared with those in the archaeal TyrRS: the recognition of the C1-G72 base pair by SceTyrRS is similar to that by the archaeal TyrRS, whereas the recognition of the A73 by SceTyrRS is different from that by the archaeal TyrRS but similar to that by the bacterial TyrRS. Thus, the lack of cross-reactivity between archaeal/eukaryotic and bacterial TyrRS-tRNA(Tyr) pairs most probably lies in the different sequence of the last base pair of the acceptor stem (C1-G72 vs G1-C72) of tRNA(Tyr). On the other hand, the recognition mode of Tyr-AMP is conserved among the TyrRSs from the three kingdoms.
Indexed as
Identifiers
What OpenQuestion holds
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.