ArticleNucleic acids research2019
The G3-U70-independent tRNA recognition by human mitochondrial alanyl-tRNA synthetase.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 28 citations in OpenAlex.
- Advances in Research onGenes · 2026Review
- In vivo structure profiling reveals human cytosolic and mitochondrial tRNA structurome and interactome in response to stress.Nature communications · 2025Article
- Eukaryotic AlaX provides multiple checkpoints for quality and quantity of aminoacyl-tRNAs in translation.Nucleic acids research · 2024Article
- 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
- Structural basis for a degenerate tRNA identity code and the evolution of bimodal specificity in human mitochondrial tRNA recognition.Nature communications · 2023Article
- The tRNA identity landscape for aminoacylation and beyond.Nucleic acids research · 2023Review
- RNA granule-clustered mitochondrial aminoacyl-tRNA synthetases form multiple complexes with the potential to fine-tune tRNA aminoacylation.Nucleic acids research · 2022Article
- Structural basis for shape-selective recognition and aminoacylation of a D-armless human mitochondrial tRNA.Nature communications · 2022Article
- Molecular basis for human mitochondrial tRNA m3C modification by alternatively spliced METTL8.Nucleic acids research · 2022Article
- Evolutionary Adjustment of tRNA Identity Rules in Bacillariophyta for Recognition by an Aminoacyl-tRNA Synthetase Adds a Facet to the Origin of Diatoms.Journal of molecular evolution · 2022Article
- Commonality and diversity in tRNA substrate recognition in t6A biogenesis by eukaryotic KEOPSs.Nucleic acids research · 2022Article
- Gain of C-Ala enables AlaRS to target the L-shaped tRNAAla.Nucleic acids research · 2022Article
- Modifications of the human tRNA anticodon loop and their associations with genetic diseases.Cellular and molecular life sciences : CMLS · 2021Review
- The uniqueness of AlaRS and its human disease connections.RNA biology · 2021Review
- Selective and competitive functions of the AAR and UPR pathways in stress-induced angiogenesis.Cell discovery · 2021Article
- Mutually exclusive substrate selection strategy by human m3C RNA transferases METTL2A and METTL6.Nucleic acids research · 2021Article
- The human tRNA taurine modification enzyme GTPBP3 is an active GTPase linked to mitochondrial diseases.Nucleic acids research · 2021Article
- A Label-Free Assay for Aminoacylation of tRNA.Genes · 2020Article
- Nitrosative stress inhibits aminoacylation and editing activities of mitochondrial threonyl-tRNA synthetase by S-nitrosation.Nucleic acids research · 2020Article
- Molecular basis for t6A modification in human mitochondria.Nucleic acids research · 2020Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alanyl-tRNA synthetases (AlaRSs) from three domains of life predominantly rely on a single wobble base pair, G3-U70, of tRNAAla as a major determinant. However, this base pair is divergent in human mitochondrial tRNAAla, but instead with a translocated G5-U68. How human mitochondrial AlaRS (hmtAlaRS) recognizes tRNAAla, in particular, in the acceptor stem region, remains unknown. In the present study, we found that hmtAlaRS is a monomer and recognizes mitochondrial tRNAAla in a G3-U70-independent manner, requiring several elements in the acceptor stem. In addition, we found that hmtAlaRS misactivates noncognate Gly and catalyzes strong transfer RNA (tRNA)-independent pre-transfer editing for Gly. A completely conserved residue outside of the editing active site, Arg663, likely functions as a tRNA translocation determinant to facilitate tRNA entry into the editing domain during editing. Finally, we investigated the effects of the severe infantile-onset cardiomyopathy-associated R592W mutation of hmtAlaRS on the canonical enzymatic activities of hmtAlaRS. Overall, our results provide fundamental information about tRNA recognition and deepen our understanding of translational quality control mechanisms by hmtAlaRS.
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