ArticleBiochemistry2007
Isolated CP1 domain of Escherichia coli leucyl-tRNA synthetase is dependent on flanking hinge motifs for amino acid editing activity.
Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 30 citations in OpenAlex.
- Cytoplasmic isoleucyl tRNA synthetase as an attractive multistage antimalarial drug target.Science translational medicine · 2023Article
- Notch4 activation aggravates NF-κB-mediated inflammation in HIV-1-associated nephropathy.Disease models & mechanisms · 2019Article
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
- tRNAs as antibiotic targets.International journal of molecular sciences · 2014Review
- Kinetic partitioning between synthetic and editing pathways in class I aminoacyl-tRNA synthetases occurs at both pre-transfer and post-transfer hydrolytic steps.The Journal of biological chemistry · 2012Article
- Yeast mitochondrial leucyl-tRNA synthetase CP1 domain has functionally diverged to accommodate RNA splicing at expense of hydrolytic editing.The Journal of biological chemistry · 2012Article
- Coordination of tRNA synthetase active sites for chemical fidelity.The Journal of biological chemistry · 2012Article
- Partitioning of tRNA-dependent editing between pre- and post-transfer pathways in class I aminoacyl-tRNA synthetases.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
- 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
- In vitro assays for the determination of aminoacyl-tRNA synthetase editing activity.Methods (San Diego, Calif.) · 2008Article
- tRNA synthetase: tRNA aminoacylation and beyond.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Protein synthesis and its fidelity rely upon the aminoacyl-tRNA synthetases. Leucyl-tRNA synthetase (LeuRS), isoleucyl-tRNA synthetase (IleRS), and valyl-tRNA synthetase (ValRS) have evolved a discrete editing domain called CP1 that hydrolyzes the respective incorrectly misaminoacylated noncognate amino acids. Although active CP1 domain fragments have been isolated for IleRS and ValRS, previous reports suggested that the LeuRS CP1 domain required idiosyncratic adaptations to confer editing activity independent of the full-length enzyme. Herein, characterization of a series of rationally designed Escherichia coli LeuRS fragments showed that the beta-strands, which link the CP1 domain to the aminoacylation core of LeuRS, are required for editing of mischarged tRNALeu. Hydrolytic activity was also enhanced by inclusion of short flexible peptides that have been called "hinges" at the end of both LeuRS beta-strands. We propose that these long beta-strand extensions of the LeuRS CP1 domain interact specifically with the tRNA for post-transfer editing of misaminoacylated amino acids.
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