ArticleNucleic acids research2002
Identification of essential domains for Escherichia coli tRNA(leu) aminoacylation and amino acid editing using minimalist RNA molecules.
Article in Nucleic acids research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Impact of tRNA-induced proline-to-serine mistranslation on the transcriptome of Drosophila melanogaster.G3 (Bethesda, Md.) · 2024Article
- Engineering tRNAs for the Ribosomal Translation of Non-proteinogenic Monomers.Chemical reviews · 2024Review
- Impact of tRNA-induced proline-to-serine mistranslation on the transcriptome ofbioRxiv : the preprint server for biology · 2024Article
- The tRNA identity landscape for aminoacylation and beyond.Nucleic acids research · 2023Review
- The 3'tsRNAs are aminoacylated: Implications for their biogenesis.PLoS genetics · 2021Article
- Reprogramming the genetic code.Nature reviews. Genetics · 2021Review
- Rapid discovery and evolution of orthogonal aminoacyl-tRNA synthetase-tRNA pairs.Nature biotechnology · 2020Article
- Aminoacyl-tRNA synthetases.RNA (New York, N.Y.) · 2020Review
- LeuRS can leucylate type I and type II tRNALeus in Streptomyces coelicolor.Nucleic acids research · 2019Article
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
- Disrupted tRNA Genes and tRNA Fragments: A Perspective on tRNA Gene Evolution.Life (Basel, Switzerland) · 2015Review
- The determination of tRNALeu recognition nucleotides for Escherichia coli L/F transferase.RNA (New York, N.Y.) · 2014Article
- Human mitochondrial leucyl tRNA synthetase can suppress non cognate pathogenic mt-tRNA mutations.EMBO molecular medicine · 2014Article
- Crucial role of the C-terminal domain of Mycobacterium tuberculosis leucyl-tRNA synthetase in aminoacylation and editing.Nucleic acids research · 2013Article
- Structural dynamics of the aminoacylation and proofreading functional cycle of bacterial leucyl-tRNA synthetase.Nature structural & molecular biology · 2012Article
- Article
- CP1-dependent partitioning of pretransfer and posttransfer editing in leucyl-tRNA synthetase.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Natural homolog of tRNA synthetase editing domain rescues conditional lethality caused by mistranslation.The Journal of biological chemistry · 2008Article
- Recognition of tRNALeu by Aquifex aeolicus leucyl-tRNA synthetase during the aminoacylation and editing steps.Nucleic acids research · 2008Article
- A Flexible peptide tether controls accessibility of a unique C-terminal RNA-binding domain in leucyl-tRNA synthetases.Journal of molecular biology · 2008Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Escherichia coli leucyl-tRNA synthetase (LeuRS) aminoacylates up to six different class II tRNA(leu) molecules. Each has a distinct anticodon and varied nucleotides in other regions of the tRNA. Attempts to construct a minihelix RNA that can be aminoacylated with leucine have been unsuccessful. Herein, we describe the smallest tRNA(leu) analog that has been aminoacylated to a significant extent to date. A series of tRNA(leu) analogs with various domains and combinations of domains deleted was constructed. The minimal RNA that was efficiently aminoacylated with LeuRS was one in which the anticodon stem-loop and variable arm stem-loop, but neither the D-arm nor T-arm, were deleted. Aminoacylation of this minimal RNA was abolished when the discriminator base A73 was replaced with C73 or when putative tertiary interactions between the D-loop and T-loop were disrupted, suggesting that these identity elements are still functioning in the minimized RNA. The various constructs that were significantly aminoacylated were also tested for amino acid editing by the synthetase. The anticodon and variable stem-loop domains were also dispensable for hydrolysis of the charged tRNA(leu) mimics. These results suggest that LeuRS may rely on identity elements in overlapping domains of the tRNA for both its aminoacylation and editing activities.
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