ArticleThe EMBO journal2005
Leucyl-tRNA synthetase from the ancestral bacterium Aquifex aeolicus contains relics of synthetase evolution.
Article in The EMBO journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed, 42 citations in OpenAlex.
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
- The Yin and Yang of tRNA: proper binding of acceptor end determines the catalytic balance of editing and aminoacylation.Nucleic acids research · 2013Article
- Kinetic proofreading at single molecular level: aminoacylation of tRNA(Ile) and the role of water as an editor.PloS one · 2013Article
- Structural phylogenomics retrodicts the origin of the genetic code and uncovers the evolutionary impact of protein flexibility.PloS one · 2013Article
- Unusual domain architecture of aminoacyl tRNA synthetases and their paralogs from Leishmania major.BMC genomics · 2012Article
- Modular pathways for editing non-cognate amino acids by human cytoplasmic leucyl-tRNA synthetase.Nucleic acids research · 2011Article
- Partitioning of tRNA-dependent editing between pre- and post-transfer pathways in class I aminoacyl-tRNA synthetases.The Journal of biological chemistry · 2010Article
- tRNA-dependent pre-transfer editing by prokaryotic leucyl-tRNA synthetase.The Journal of biological chemistry · 2010Article
- A genomic glimpse of aminoacyl-tRNA synthetases in malaria parasite Plasmodium falciparum.BMC genomics · 2009Article
- A paradigm shift for the amino acid editing mechanism of human cytoplasmic leucyl-tRNA synthetase.Biochemistry · 2009Article
- Defects in transient tRNA translocation bypass tRNA synthetase quality control mechanisms.The Journal of biological chemistry · 2009Article
- The CP2 domain of leucyl-tRNA synthetase is crucial for amino acid activation and post-transfer editing.The Journal of biological chemistry · 2008Article
- 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
- Recognition of tRNALeu by Aquifex aeolicus leucyl-tRNA synthetase during the aminoacylation and editing steps.Nucleic acids research · 2008Article
- In vitro assays for the determination of aminoacyl-tRNA synthetase editing activity.Methods (San Diego, Calif.) · 2008Article
- Isolated CP1 domain of Escherichia coli leucyl-tRNA synthetase is dependent on flanking hinge motifs for amino acid editing activity.Biochemistry · 2007Article
- A present-day aminoacyl-tRNA synthetase with ancestral editing properties.RNA (New York, N.Y.) · 2007Article
- Crystal structures of the editing domain of Escherichia coli leucyl-tRNA synthetase and its complexes with Met and Ile reveal a lock-and-key mechanism for amino acid discrimination.The Biochemical journal · 2006Article
- Crystallization and preliminary X-ray crystallographic study of the wild type and two mutants of the CP1 hydrolytic domain from Aquifex aeolicus leucyl-tRNA synthetase.Acta crystallographica. Section F, Structural biology and crystallization communications · 2005Article
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The editing reactions catalyzed by aminoacyl-tRNA synthetases are critical for the faithful protein synthesis by correcting misactivated amino acids and misaminoacylated tRNAs. We report that the isolated editing domain of leucyl-tRNA synthetase from the deep-rooted bacterium Aquifex aeolicus (alphabeta-LeuRS) catalyzes the hydrolytic editing of both mischarged tRNA(Leu) and minihelix(Leu). Within the domain, we have identified a crucial 20-amino-acid peptide that confers editing capacity when transplanted into the inactive Escherichia coli LeuRS editing domain. Likewise, fusion of the beta-subunit of alphabeta-LeuRS to the E. coli editing domain activates its editing function. These results suggest that alphabeta-LeuRS still carries the basic features from a primitive synthetase molecule. It has a remarkable capacity to transfer autonomous active modules, which is consistent with the idea that modern synthetases arose after exchange of small idiosyncratic domains. It also has a unique alphabeta-heterodimeric structure with separated catalytic and tRNA-binding sites. Such an organization supports the tRNA/synthetase coevolution theory that predicts sequential addition of tRNA and synthetase domains.
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