ArticleRNA (New York, N.Y.)2007
A present-day aminoacyl-tRNA synthetase with ancestral editing properties.
Article in RNA (New York, N.Y.), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- The role of tRNA identity elements in aminoacyl-tRNA editing.Frontiers in microbiology · 2024Review
- Acetylation of lysine ϵ-amino groups regulates aminoacyl-tRNA synthetase activity inThe Journal of biological chemistry · 2017Article
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
- A bridge between the aminoacylation and editing domains of leucyl-tRNA synthetase is crucial for its synthetic activity.RNA (New York, N.Y.) · 2014Article
- Norvaline and norleucine may have been more abundant protein components during early stages of cell evolution.Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life · 2013Review
- In vivo identification of essential nucleotides in tRNALeu to its functions by using a constructed yeast tRNALeu knockout strain.Nucleic acids research · 2012Article
- Do anticodons of misacylated tRNAs preferentially mismatch codons coding for the misloaded amino acid?BMC molecular biology · 2010Article
- One ancestor for two codes viewed from the perspective of two complementary modes of tRNA aminoacylation.Biology direct · 2009Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Leucyl-, isoleucyl-, and valyl-tRNA synthetases form a subgroup of related aminoacyl-tRNA synthetases that attach similar amino acids to their cognate tRNAs. To prevent amino acid misincorporation during translation, these enzymes also hydrolyze mischarged tRNAs through a post-transfer editing mechanism. Here we show that LeuRS from the deep-branching bacterium Aquifex aeolicus edits the complete set of aminoacylated tRNAs generated by the three enzymes: Ile-tRNA(Ile), Val-tRNA(Ile), Val-tRNA(Val), Thr-tRNA(Val), and Ile-tRNA(Leu). This unusual enlarged editing property was studied in a model of a primitive editing system containing a composite minihelix carrying the triple leucine, isoleucine, and valine identity mimicking the primitive tRNA precursor. We found that the freestanding LeuRS editing domain can edit this precursor in contrast to IleRS and ValRS editing domains. These results suggest that A. aeolicus LeuRS carries editing properties that seem more primitive than those of IleRS and ValRS. They suggest that the A. aeolicus editing domain has preserved the ambiguous editing property from the ancestral common editing domain or, alternatively, that this plasticity results from a specific metabolic adaptation.
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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.