| Autor: |
Claus A. Schmitz, María del Mar Carretero, Stacy Hovde, Maria Solà-Vilarrubias, Philip A. Knobel, Merve Nur Güler, Eva Maria Novoa, Marta Rodríguez-Escribà, Alba Serrano, Lluís Ribas de Pouplana, Travis H. Stracker, Noelia Camacho, Daria Picchioni, Antigoni Machallekidou, Laurie S. Kaguni, Alba Pons-Pons, Albert Antolin-Fontes |
| Rok vydání: |
2018 |
| Předmět: |
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| Zdroj: |
SSRN Electronic Journal. |
| ISSN: |
1556-5068 |
| Popis: |
The aminoacylation of tRNAs by aminoacyl-tRNA synthetases (ARS) is a central reaction in biology. Multiple regulatory pathways utilize the aminoacylation status of cytosolic tRNAs to monitor and regulate metabolism. The existence of equivalent regulatory networks within the mitochondria is unknown. Here we describe a functional network that couples protein synthesis to DNA replication in animal mitochondria. We show that a duplication of the gene coding for mitochondrial seryl-tRNA synthetase (SerRS2) generated a paralog protein (SLIMP) in arthropods that forms a heterodimeric complex with a SerRS2 monomer. This seryl-tRNA synthetase variant is essential for protein synthesis and mitochondrial respiration. In addition, SLIMP interacts with the substrate binding domain of the mitochondrial protease LON, thus stimulating proteolysis of the DNA-binding protein TFAM, and repressing mitochondrial DNA (mtDNA) replication. Thus, mitochondrial translation is directly coupled to mtDNA replication by a network based upon a profound structural modification of an animal ARS. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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