Plant-Specific Preprotein and Amino Acid Transporter Proteins Are Required for tRNA Import into Mitochondria
Autor: | Jürgen Soll, Beata Kmiec, Annette Schock, Sabrina Kraus, Szymon Kubiszewski-Jakubiak, Aneta Ivanova, Katrin Philippar, Oliver Berkowitz, Pedro Teixeira, Cyrille Megel, Reena Narsai, E. Glaser, Monika W. Murcha, James Whelan, Laurence Maréchal-Drouard, Irene L. Gügel |
---|---|
Přispěvatelé: | Institut de biologie moléculaire des plantes (IBMP), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA) |
Jazyk: | angličtina |
Rok vydání: | 2016 |
Předmět: |
0301 basic medicine
Alanine Physiology Translation (biology) [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biology Plant Science Mitochondrion Biology biology.organism_classification 03 medical and health sciences 030104 developmental biology Biochemistry Arabidopsis Transfer RNA Gene expression Genetics Protein biosynthesis Arabidopsis thaliana [SDV.BV]Life Sciences [q-bio]/Vegetal Biology tRNA |
Zdroj: | Plant Physiology Plant Physiology, American Society of Plant Biologists, 2016, 172 (4), pp.2471-2490. ⟨10.1104/pp.16.01519⟩ |
ISSN: | 0032-0889 1532-2548 |
DOI: | 10.1104/pp.16.01519⟩ |
Popis: | A variety of eukaryotes, in particular plants, do not contain the required number of tRNAs to support the translation of mitochondria-encoded genes and thus need to import tRNAs from the cytosol. This study identified two Arabidopsis (Arabidopsis thaliana) proteins, Tric1 and Tric2 (for tRNA import component), which on simultaneous inactivation by T-DNA insertion lines displayed a severely delayed and chlorotic growth phenotype and significantly reduced tRNA import capacity into isolated mitochondria. The predicted tRNA-binding domain of Tric1 and Tric2, a sterile-α-motif at the C-terminal end of the protein, was required to restore tRNA uptake ability in mitochondria of complemented plants. The purified predicted tRNA-binding domain binds the T-arm of the tRNA for alanine with conserved lysine residues required for binding. T-DNA inactivation of both Tric proteins further resulted in an increase in the in vitro rate of in organello protein synthesis, which was mediated by a reorganization of the nuclear transcriptome, in particular of genes encoding a variety of proteins required for mitochondrial gene expression at both the transcriptional and translational levels. The characterization of Tric1/2 provides mechanistic insight into the process of tRNA import into mitochondria and supports the theory that the tRNA import pathway resulted from the repurposing of a preexisting protein import apparatus. |
Databáze: | OpenAIRE |
Externí odkaz: |