ArticleThe Journal of biological chemistry2012
Yeast mitochondrial leucyl-tRNA synthetase CP1 domain has functionally diverged to accommodate RNA splicing at expense of hydrolytic editing.
Article in The Journal of biological chemistry, 2012. 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.
- Moonlighting Proteins: Diverse Functions Found in Fungi.Journal of fungi (Basel, Switzerland) · 2023Review
- Seryl-tRNA Synthetase Shows a Noncanonical Activity of Upregulating Laccase Transcription inMicrobiology spectrum · 2023Article
- Exploring the Ability of LARS2 Carboxy-Terminal Domain in Rescuing the MELAS Phenotype.Life (Basel, Switzerland) · 2021Article
- Review
- Moonlighting Proteins in the Fuzzy Logic of Cellular Metabolism.Molecules (Basel, Switzerland) · 2020Review
- Error-prone protein synthesis in parasites with the smallest eukaryotic genome.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Article
- LARS2 Variants Associated with Hydrops, Lactic Acidosis, Sideroblastic Anemia, and Multisystem Failure.JIMD reports · 2016Article
- Caenorhabditis elegans glp-4 Encodes a Valyl Aminoacyl tRNA Synthetase.G3 (Bethesda, Md.) · 2015Article
- Degenerate connective polypeptide 1 (CP1) domain from human mitochondrial leucyl-tRNA synthetase.The Journal of biological chemistry · 2015Article
- Human mitochondrial leucyl tRNA synthetase can suppress non cognate pathogenic mt-tRNA mutations.EMBO molecular medicine · 2014Article
- Emergence and evolution.Topics in current chemistry · 2014Review
- An insertion peptide in yeast glycyl-tRNA synthetase facilitates both productive docking and catalysis of cognate tRNAs.Molecular and cellular biology · 2013Article
- Essential nontranslational functions of tRNA synthetases.Nature chemical biology · 2013Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The yeast mitochondrial leucyl-tRNA synthetase (ymLeuRS) performs dual essential roles in group I intron splicing and protein synthesis. A specific LeuRS domain called CP1 is responsible for clearing noncognate amino acids that are misactivated during aminoacylation. The ymLeuRS CP1 domain also plays a critical role in splicing. Herein, the ymLeuRS CP1 domain was isolated from the full-length enzyme and was active in RNA splicing in vitro. Unlike its Escherichia coli LeuRS CP1 domain counterpart, it failed to significantly hydrolyze misaminoacylated tRNA(Leu). In addition and in stark contrast to the yeast domain, the editing-active E. coli LeuRS CP1 domain failed to recapitulate the splicing activity of the full-length E. coli enzyme. Although LeuRS-dependent splicing activity is rooted in an ancient adaptation for its aminoacylation activity, these results suggest that the ymLeuRS has functionally diverged to confer a robust splicing activity. This adaptation could have come at some expense to the protein's housekeeping role in aminoacylation and editing.
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