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

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dc.contributor.author Picchioni, Daria
dc.contributor.author Antolin-Fontes, Albert
dc.contributor.author Camacho, Noelia
dc.contributor.author Schmitz, Claus
dc.contributor.author Pons-Pons, Alba
dc.contributor.author Rodríguez-Escribà, Marta
dc.contributor.author Machallekidou, Antoni
dc.contributor.author Güler, Merve Nur
dc.contributor.author Siatra, Panagiota
dc.contributor.author Carretero-Junquera, Maria
dc.contributor.author Serrano, Alba
dc.contributor.author Hovde, Stacy L.
dc.contributor.author Knobel, Philip A.
dc.contributor.author Novoa, Eva Maria
dc.contributor.author Solà-Vilarrubias, Maria
dc.contributor.author Kaguni, Laurie S.
dc.contributor.author Stracker, Travis
dc.contributor.author Ribas de Pouplana, Lluís
dc.date.accessioned 2019-07-16T09:27:19Z
dc.date.available 2019-07-16T09:27:19Z
dc.date.issued 2019
dc.identifier.citation Picchioni D, Antolin-Fontes A, Camacho N, Schmitz C, Pons-Pons A, Rodríguez-Escribà M et al. Mitochondrial protein synthesis and mtDNA levels coordinated through an aminoacyl-tRNA synthetase subunit. Cell Rep. 2019 Apr 2; 27(1): 40-47.e5. DOIi: 10.1016/j.celrep.2019.03.022
dc.identifier.issn 2211-1247
dc.identifier.uri http://hdl.handle.net/10230/42003
dc.description.abstract 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.
dc.description.sponsorship This work was supported by grants SVP2014-068398 and BIO2015-64572 from the Spanish Ministry of Economy and Competitiveness (to L.R.d.P.). This work used the platforms of the Grenoble Instruct Centre (ISBG; UMS 3518 CNRS-CEA-UJF-EMBL) with support from FRISBI (ANR-10-INSB-05-02) and GRAL (ANR-10-LABX-49-01) within the Grenoble Partnership for Structural Biology (PSB)
dc.format.mimetype application/pdf
dc.language.iso eng
dc.publisher Elsevier
dc.rights © 2019 The Authors. This is an open access article under a CC BY-NC-ND license
dc.rights.uri https://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subject.other Mitocondris
dc.subject.other ADN mitocondrial
dc.subject.other RNA
dc.title Mitochondrial protein synthesis and mtDNA levels coordinated through an aminoacyl-tRNA synthetase subunit
dc.type info:eu-repo/semantics/article
dc.identifier.doi http://dx.doi.org/10.1016/j.celrep.2019.03.022
dc.relation.projectID info:eu-repo/grantAgreement/ES/1PE/SVP2014-068398
dc.relation.projectID info:eu-repo/grantAgreement/ES/1PE/BIO2015-64572
dc.rights.accessRights info:eu-repo/semantics/openAccess
dc.type.version info:eu-repo/semantics/publishedVersion


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