Mitochondrial Protein Synthesis and mtDNA Levels Coordinated through an Aminoacyl-tRNA Synthetase Subunit.
LON
mitochondria
mtDNA
replication
seryl-tRNA synthetase
tRNA
translation
Journal
Cell reports
ISSN: 2211-1247
Titre abrégé: Cell Rep
Pays: United States
ID NLM: 101573691
Informations de publication
Date de publication:
02 04 2019
02 04 2019
Historique:
received:
03
12
2018
revised:
13
02
2019
accepted:
06
03
2019
entrez:
4
4
2019
pubmed:
4
4
2019
medline:
2
6
2020
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 30943413
pii: S2211-1247(19)30329-8
doi: 10.1016/j.celrep.2019.03.022
pii:
doi:
Substances chimiques
DNA, Mitochondrial
0
Drosophila Proteins
0
Mitochondrial Proteins
0
Protein Subunits
0
Amino Acyl-tRNA Synthetases
EC 6.1.1.-
SLIMP protein, Drosophila
EC 6.1.1.11
SerRS protein, Drosophila
EC 6.1.1.11
Serine-tRNA Ligase
EC 6.1.1.11
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
40-47.e5Informations de copyright
Copyright © 2019 The Authors. Published by Elsevier Inc. All rights reserved.