ArticleProceedings of the National Academy of Sciences of the United States of America2005
Dual targeting is the rule for organellar aminoacyl-tRNA synthetases in Arabidopsis thaliana.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.
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Who cites it
110 citing papers in PubMed, 248 citations in OpenAlex.
- From water to land: evolution of tRNA gene repertoires in photosynthetic organisms.The EMBO journal · 2026Review
- Discovery of regulatory complexes in Arabidopsis via protein-metabolite mapping during Pseudomonas infection.Plant physiology · 2026Article
- The Effects of Rapid Mitochondrial Gene Loss on Organellar Proteomes.Genome biology and evolution · 2026Article
- Reshaping organellar translation and tRNA metabolism: the consequences of photosynthesis loss and massive horizontal gene transfer.Molecular biology and evolution · 2026Article
- Fungal-Derived tRNAs Are Expressed and Aminoacylated in Orchid Mitochondria.Molecular biology and evolution · 2025Article
- Dual Roles of Reducing Systems in Protein Persulfidation and Depersulfidation.Antioxidants (Basel, Switzerland) · 2025Review
- Photosynthetic demands on translational machinery drive retention of redundant tRNA metabolism in plant organelles.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- AARS Online: A collaborative database on the structure, function, and evolution of the aminoacyl-tRNA synthetases.IUBMB life · 2024Article
- Review
- Article
- How do bacterial endosymbionts work with so few genes?PLoS biology · 2024Article
- Multi-Omics Analysis Revealed thePlants (Basel, Switzerland) · 2024Article
- 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
- Rewiring of Aminoacyl-tRNA Synthetase Localization and Interactions in Plants With Extensive Mitochondrial tRNA Gene Loss.Molecular biology and evolution · 2023Article
- Aminoacyl-tRNA Synthetase Evolution within the Dynamic Tripartite Translation System of Plant Cells.Genome biology and evolution · 2023Article
- Coordinated regulation of the mitochondrial retrograde response by circadian clock regulators and ANAC017.Plant communications · 2023Article
- Translation in Mitochondrial Ribosomes.Methods in molecular biology (Clifton, N.J.) · 2023Article
- The tomato chloroplast stromal proteome compendium elucidated by leveraging a plastid protein-localization prediction Atlas.Frontiers in plant science · 2023Article
- Mechanisms governing codon usage bias and the implications for protein expression in the chloroplast of Chlamydomonas reinhardtii.The Plant journal : for cell and molecular biology · 2022Review
50 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In plants, protein synthesis occurs in the cytosol, mitochondria, and plastids. Each compartment requires a full set of tRNAs and aminoacyl-tRNA synthetases. We have undertaken a systematic analysis of the targeting of organellar aminoacyl-tRNA synthetases in the model plant Arabidopsis thaliana. Dual targeting appeared to be a general rule. Among the 24 identified organellar aminoacyl-tRNA synthetases (aaRSs), 15 (and probably 17) are shared between mitochondria and plastids, and 5 are shared between cytosol and mitochondria (one of these aaRSs being present also in chloroplasts). Only two were shown to be uniquely chloroplastic and none to be uniquely mitochondrial. Moreover, there are no examples where the three aaRS genes originating from the three ancestral genomes still coexist. These results indicate that extensive exchange of aaRSs has occurred during evolution and that many are now shared between two or even three compartments. The findings have important implications for studies of the translation machinery in plants and on protein targeting and gene transfer in general.
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