Expression of nuclear and mitochondrial genes encoding ATP synthase is synchronized by disassembly of a multisynthetase complex.
Fiche publication
Date publication
décembre 2014
Journal
Molecular cell
Auteurs
Membres identifiés du Cancéropôle Est :
Mr HAMMANN Philippe
Tous les auteurs :
Frechin M, Enkler L, Tetaud E, Laporte D, Senger B, Blancard C, Hammann P, Bader G, Clauder-Münster S, Steinmetz LM, Martin RP, di Rago JP, Becker HD
Lien Pubmed
Résumé
In eukaryotic cells, oxidative phosphorylation involves multisubunit complexes of mixed genetic origin. Assembling these complexes requires an organelle-independent synchronizing system for the proper expression of nuclear and mitochondrial genes. Here we show that proper expression of the F1FO ATP synthase (complex V) depends on a cytosolic complex (AME) made of two aminoacyl-tRNA synthetases (cERS and cMRS) attached to an anchor protein, Arc1p. When yeast cells adapt to respiration the Snf1/4 glucose-sensing pathway inhibits ARC1 expression triggering simultaneous release of cERS and cMRS. Free cMRS and cERS relocate to the nucleus and mitochondria, respectively, to synchronize nuclear transcription and mitochondrial translation of ATP synthase genes. Strains releasing asynchronously the two aminoacyl-tRNA synthetases display aberrant expression of nuclear and mitochondrial genes encoding subunits of complex V resulting in severe defects of the oxidative phosphorylation mechanism. This work shows that the AME complex coordinates expression of enzymes that require intergenomic control.
Mots clés
Cell Nucleus, genetics, Gene Expression, Gene Expression Regulation, Fungal, Mitochondria, genetics, Multienzyme Complexes, Protein Multimerization, Proton-Translocating ATPases, genetics, RNA-Binding Proteins, physiology, Saccharomyces cerevisiae, enzymology, Saccharomyces cerevisiae Proteins, physiology
Référence
Mol. Cell. 2014 Dec;56(6):763-76