tRNA-Dependent Import of a Transit Sequence-Less Aminoacyl-tRNA Synthetase (LeuRS2) into the Mitochondria of Arabidopsis
| Autor: | Steffen Reinbothe, Diter von Wettstein, Claudia Rossig, Sachin Rustgi, John Gray, Christiane Reinbothe, Joachim Rassow |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
0106 biological sciences
0301 basic medicine Mitochondrial DNA Arabidopsis Mitochondrion 01 natural sciences Article Catalysis lcsh:Chemistry Inorganic Chemistry Mitochondrial Proteins 03 medical and health sciences chemistry.chemical_compound RNA Transfer transit sequence-less precursors Physical and Theoretical Chemistry lcsh:QH301-705.5 Molecular Biology Spectroscopy Plant Proteins Organelle Biogenesis PRAT proteins Chemistry Aminoacyl tRNA synthetase Organic Chemistry Translation (biology) Biological Transport General Medicine Computer Science Applications Transport protein Mitochondria cell death 030104 developmental biology lcsh:Biology (General) lcsh:QD1-999 Mitochondrial biogenesis Biochemistry Transfer RNA Mutation protein transport Leucine-tRNA Ligase Sterile alpha motif 010606 plant biology & botany Protein Binding |
| Zdroj: | International Journal of Molecular Sciences Volume 22 Issue 8 International Journal of Molecular Sciences, Vol 22, Iss 3808, p 3808 (2021) |
| ISSN: | 1422-0067 |
| Popis: | Aminoacyl-tRNA synthetases (AaRS) charge tRNAs with amino acids for protein translation. In plants, cytoplasmic, mitochondrial, and chloroplast AaRS exist that are all coded for by nuclear genes and must be imported from the cytosol. In addition, only a few of the mitochondrial tRNAs needed for translation are encoded in mitochondrial DNA. Despite considerable progress made over the last few years, still little is known how the bulk of cytosolic AaRS and respective tRNAs are transported into mitochondria. Here, we report the identification of a protein complex that ties AaRS and tRNA import into the mitochondria of Arabidopsis thaliana. Using leucyl-tRNA synthetase 2 (LeuRS2) as a model for a mitochondrial signal peptide (MSP)-less precursor, a ≈30 kDa protein was identified that interacts with LeuRS2 during import. The protein identified is identical with a previously characterized mitochondrial protein designated HP30-2 (encoded by At3g49560) that contains a sterile alpha motif (SAM) similar to that found in RNA binding proteins. HP30-2 is part of a larger protein complex that contains with TIM22, TIM8, TIM9 and TIM10 four previously identified components of the translocase for MSP-less precursors. Lack of HP30-2 perturbed mitochondrial biogenesis and function and caused seedling lethality during greening, suggesting an essential role of HP30-2 in planta. |
| Databáze: | OpenAIRE |
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