ArticleRNA (New York, N.Y.)2003
Recognition of acceptor-stem structure of tRNA(Asp) by Escherichia coli aspartyl-tRNA synthetase.
Article in RNA (New York, N.Y.), 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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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.
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.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- tRNA engineering strategies for genetic code expansion.Frontiers in genetics · 2024Review
- Modification of Transfer RNA Levels Affects Cyclin Aggregation and the Correct Duplication of Yeast Cells.Frontiers in microbiology · 2020Article
- Naturally occurring dual recognition of tRNARNA biology · 2019Article
- Emergence of a "Cyclosome" in a Primitive Network Capable of Building "Infinite" Proteins.Life (Basel, Switzerland) · 2019Article
- The RNA chaperone La promotes pre-tRNA maturation via indiscriminate binding of both native and misfolded targets.Nucleic acids research · 2017Article
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
- Plasmodial aspartyl-tRNA synthetases and peculiarities in Plasmodium falciparum.The Journal of biological chemistry · 2009Article
- Global responses of Methanococcus maripaludis to specific nutrient limitations and growth rate.Journal of bacteriology · 2008Article
- Surprising contribution to aminoacylation and translation of non-Watson-Crick pairs in tRNA.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- A truncated aminoacyl-tRNA synthetase modifies RNA.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Aminoacylation properties of pathology-related human mitochondrial tRNA(Lys) variants.RNA (New York, N.Y.) · 2004Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Protein-RNA recognition between aminoacyl-tRNA synthetases and tRNA is highly specific and essential for cell viability. We investigated the structure-function relationships involved in the interaction of the Escherichia coli tRNA(Asp) acceptor stem with aspartyl-tRNA synthetase. The goal was to isolate functionally active mutants and interpret them in terms of the crystal structure of the synthetase-tRNA(Asp) complex. Mutants were derived from Saccharomyces cerevisiae tRNA(Asp), which is inactive with E. coli aspartyl-tRNA synthetase, allowing a genetic selection of active tRNAs in a tRNA(Asp) knockout strain of E. coli. The mutants were obtained by directed mutagenesis or library selections that targeted the acceptor stem of the yeast tRNA(Asp) gene. The mutants provide a rich source of tRNA(Asp) sequences, which show that the sequence of the acceptor stem can be extensively altered while allowing the tRNA to retain substantial aminoacylation and cell-growth functions. The predominance of tRNA backbone-mediated interactions observed between the synthetase and the acceptor stem of the tRNA in the crystal and the mutability of the acceptor stem suggest that many of the corresponding wild-type bases are replaceable by alternative sequences, so long as they preserve the initial backbone structure of the tRNA. Backbone interactions emerge as an important functional component of the tRNA-synthetase interaction.
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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.