ArticleNucleic acids research2011
Modular pathways for editing non-cognate amino acids by human cytoplasmic leucyl-tRNA synthetase.
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 52 citations in OpenAlex.
- Animal amino acid sensor - A review.Animal bioscience · 2025Article
- Mammalian mitochondrial translation infidelity leads to oxidative stress-induced cell cycle arrest and cardiomyopathy.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Co-ingestion of glutamine and leucine synergistically promotes mTORC1 activation.Scientific reports · 2022Article
- Amino Acids in Autophagy: Regulation and Function.Advances in experimental medicine and biology · 2021Article
- Amino Acids in Cell Signaling: Regulation and Function.Advances in experimental medicine and biology · 2021Article
- Molecular basis of the multifaceted functions of human leucyl-tRNA synthetase in protein synthesis and beyond.Nucleic acids research · 2020Article
- Review
- Sestrins at the Interface of ROS Control and Autophagy Regulation in Health and Disease.Oxidative medicine and cellular longevity · 2019Review
- Leishmania donovani Parasites Are Inhibited by the Benzoxaborole AN2690 Targeting Leucyl-tRNA Synthetase.Antimicrobial agents and chemotherapy · 2018Article
- 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
- The Dawn of the Age of Amino Acid Sensors for the mTORC1 Pathway.Cell metabolism · 2017Review
- [Clinical feature and molecular diagnostic analysis of the first non-caucasian child with infantile liver failure syndrome type 1].Zhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics · 2017Article
- Self-protective responses to norvaline-induced stress in a leucyl-tRNA synthetase editing-deficient yeast strain.Nucleic acids research · 2017Article
- Recent Advances in Understanding Amino Acid Sensing Mechanisms that Regulate mTORC1.International journal of molecular sciences · 2016Review
- Multiple Quality Control Pathways Limit Non-protein Amino Acid Use by Yeast Cytoplasmic Phenylalanyl-tRNA Synthetase.The Journal of biological chemistry · 2016Article
- Biochemical Basis of Sestrin Physiological Activities.Trends in biochemical sciences · 2016Review
- Sestrin regulation of TORC1: Is Sestrin a leucine sensor?Science signaling · 2016Review
- C-terminal Domain of Leucyl-tRNA Synthetase from Pathogenic Candida albicans Recognizes both tRNASer and tRNALeu.The Journal of biological chemistry · 2016Article
- Sestrin2 is a leucine sensor for the mTORC1 pathway.Science (New York, N.Y.) · 2016Article
- Degenerate connective polypeptide 1 (CP1) domain from human mitochondrial leucyl-tRNA synthetase.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To prevent potential errors in protein synthesis, some aminoacyl-transfer RNA (tRNA) synthetases have evolved editing mechanisms to hydrolyze misactivated amino acids (pre-transfer editing) or misacylated tRNAs (post-transfer editing). Class Ia leucyl-tRNA synthetase (LeuRS) may misactivate various natural and non-protein amino acids and then mischarge tRNA(Leu). It is known that the fidelity of prokaryotic LeuRS depends on multiple editing pathways to clear the incorrect intermediates and products in the every step of aminoacylation reaction. Here, we obtained human cytoplasmic LeuRS (hcLeuRS) and tRNA(Leu) (hctRNA(Leu)) with high activity from Escherichia coli overproducing strains to study the synthetic and editing properties of the enzyme. We revealed that hcLeuRS could adjust its editing strategy against different non-cognate amino acids. HcLeuRS edits norvaline predominantly by post-transfer editing; however, it uses mainly pre-transfer editing to edit α-amino butyrate, although both amino acids can be charged to tRNA(Leu). Post-transfer editing as a final checkpoint of the reaction was very important to prevent mis-incorporation in vitro. These results provide insight into the modular editing pathways created to prevent genetic code ambiguity by evolution.
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