Yeast mitochondrial Gln-tRNAGln is generated by a GatFAB-mediated transamidation pathway involving Arc1p-controlled subcellular sorting of cytosolic GluRS
| Autor: | Robert P. Martin, Daniel Kern, Mélanie Brayé, Hubert Dominique Becker, Bruno Senger, Mathieu Frechin |
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| Přispěvatelé: | Architecture et Réactivité de l'ARN (ARN), Institut de biologie moléculaire et cellulaire (IBMC), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Génétique moléculaire, génomique, microbiologie (GMGM), 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: | 2009 |
| Předmět: |
Cytoplasm
[SDV]Life Sciences [q-bio] Plasma protein binding RNA Transfer Amino Acyl Mitochondrion MESH: Saccharomyces cerevisiae Proteins Gene Expression Regulation Fungal ComputingMilieux_MISCELLANEOUS 0303 health sciences tRNA-dependent amidotransferase MESH: Glutamate-tRNA Ligase biology 030302 biochemistry & molecular biology RNA-Binding Proteins MESH: Glutamic Acid MESH: Saccharomyces cerevisiae Transport protein mitochondria Protein Transport Biochemistry Transfer RNA MESH: Gene Expression Regulation Fungal Protein Binding Research Paper MESH: Protein Transport Saccharomyces cerevisiae Proteins MESH: Mitochondria Saccharomyces cerevisiae Glutamic Acid [SDV.BC]Life Sciences [q-bio]/Cellular Biology 03 medical and health sciences Dual localization tRNAGln Transferases MESH: Transferases MESH: RNA Transfer Amino Acyl Genetics MESH: Protein Binding [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Nuclear export signal 030304 developmental biology Glutamine amidotransferase MESH: Cytoplasm biology.organism_classification Glutamate-tRNA Ligase Cytosol MESH: RNA-Binding Proteins metabolism Developmental Biology |
| Zdroj: | Genes and Development Genes and Development, Cold Spring Harbor Laboratory Press, 2009, 23 (9), pp.1119-1130. ⟨10.1101/gad.518109⟩ Genes and Development, Cold Spring Harbor Laboratory Press, 2009, 23 (9), pp.1119-30. ⟨10.1101/gad.518109⟩ |
| ISSN: | 0890-9369 |
| DOI: | 10.1101/gad.518109⟩ |
| Popis: | It is impossible to predict which pathway, direct glutaminylation of tRNAGln or tRNA-dependent transamidation of glutamyl-tRNAGln, generates mitochondrial glutaminyl-tRNAGln for protein synthesis in a given species. The report that yeast mitochondria import both cytosolic glutaminyl-tRNA synthetase and tRNAGln has challenged the widespread use of the transamidation pathway in organelles. Here we demonstrate that yeast mitochondrial glutaminyl-tRNAGln is in fact generated by a transamidation pathway involving a novel type of trimeric tRNA-dependent amidotransferase (AdT). More surprising is the fact that cytosolic glutamyl-tRNA synthetase (cERS) is imported into mitochondria, where it constitutes the mitochondrial nondiscriminating ERS that generates the mitochondrial mischarged glutamyl-tRNAGln substrate for the AdT. We show that dual localization of cERS is controlled by binding to Arc1p, a tRNA nuclear export cofactor that behaves as a cytosolic anchoring platform for cERS. Expression of Arc1p is down-regulated when yeast cells are switched from fermentation to respiratory metabolism, thus allowing increased import of cERS to satisfy a higher demand of mitochondrial glutaminyl-tRNAGln for mitochondrial protein synthesis. This novel strategy that enables a single protein to be localized in both the cytosol and mitochondria provides a new paradigm for regulation of the dynamic subcellular distribution of proteins between membrane-separated compartments. |
| Databáze: | OpenAIRE |
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