Mitochondrial protein synthesis and mtDNA levels coordinated through an aminoacyl-tRNA synthetase subunit

The aminoacylation of tRNAs by aminoacyl-tRNA synthetases (ARSs) is a central reaction in biology. Multiple regulatory pathways use the aminoacylation status of cytosolic tRNAs to monitor and regulate metabolism. The existence of equivalent regulatory networks within the mitochondria is unknown. Her...

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Detalhes bibliográficos
Autores: Picchioni, Daria, Antolin-Fontes, Albert, Camacho, Noelia, Schmitz, Claus, Pons-Pons, Alba, Rodríguez-Escribà, Marta, Machallekidou, Antoni, Güler, Merve Nur, Siatra, Panagiota, Carretero-Junquera, Maria, Serrano, Alba, Hovde, Stacy L., Knobel, Philip A., Novoa, Eva Maria, Solà-Vilarrubias, Maria, Kaguni, Laurie S., Stracker, Travis, Ribas de Pouplana, Lluís
Tipo de documento: artigo
Estado:Versão publicada
Data de publicação:2019
País:España
Recursos:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositório:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:10230/42003
Acesso em linha:http://hdl.handle.net/10230/42003
http://dx.doi.org/10.1016/j.celrep.2019.03.022
Access Level:Acceso aberto
Palavra-chave:Mitocondris
ADN mitocondrial
RNA
Descrição
Resumo:The aminoacylation of tRNAs by aminoacyl-tRNA synthetases (ARSs) is a central reaction in biology. Multiple regulatory pathways use 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 in arthropods a paralog protein (SLIMP) 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 preventing mitochondrial DNA (mtDNA) accumulation. Thus, mitochondrial translation is directly coupled to mtDNA levels by a network based upon a profound structural modification of an animal ARS.

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