ArticleNature communications2022
Structural basis for shape-selective recognition and aminoacylation of a D-armless human mitochondrial tRNA.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 20 citations in OpenAlex.
- Comparative Mitogenome Analyses Uncover Mitogenome Features and Phylogenetic Implications of the Rabbitfishes (Perciformes: Siganidae).Ecology and evolution · 2026Article
- Substrate selectivity of the human RNA mNature · 2026Article
- Mitochondrial tRNAHuman mutation · 2026Article
- Article
- Architecture ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Molecular basis of human nuclear and mitochondrial tRNA 3' processing.Nature structural & molecular biology · 2025Article
- Evolving Escherichia coli to use a tRNA with a non-canonical fold as an adaptor of the genetic code.Nucleic acids research · 2024Article
- The Complete Mitochondrial Genome of the Siberian ScoterInternational journal of molecular sciences · 2024Article
- Eukaryotic AlaX provides multiple checkpoints for quality and quantity of aminoacyl-tRNAs in translation.Nucleic acids research · 2024Article
- The human mitochondrial mRNA structurome reveals mechanisms of gene expression.Science (New York, N.Y.) · 2024Article
- Recognition of the tRNA structure: Everything everywhere but not all at once.Cell chemical biology · 2024Review
- Protein-Protein Interactions of Seryl-tRNA Synthetases with Emphasis on Human Counterparts and Their Connection to Health and Disease.Life (Basel, Switzerland) · 2024Review
- Domain collapse and active site ablation generate a widespread animal mitochondrial seryl-tRNA synthetase.Nucleic acids research · 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
- The binding mode of orphan glycyl-tRNA synthetase with tRNA supports the synthetase classification and reveals large domain movements.Science advances · 2023Article
- Selective degradation of tRNASer(AGY) is the primary driver for mitochondrial seryl-tRNA synthetase-related disease.Nucleic acids research · 2022Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Human mitochondrial gene expression relies on the specific recognition and aminoacylation of mitochondrial tRNAs (mtRNAs) by nuclear-encoded mitochondrial aminoacyl-tRNA synthetases (mt-aaRSs). Despite their essential role in cellular energy homeostasis, strong mutation pressure and genetic drift have led to an unparalleled sequence erosion of animal mtRNAs. The structural and functional consequences of this erosion are not understood. Here, we present cryo-EM structures of the human mitochondrial seryl-tRNA synthetase (mSerRS) in complex with mtRNA
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