Expression of nuclear and mitochondrial genes encoding ATP synthase is synchronized by disassembly of a multisynthetase complex

Mol Cell. 2014 Dec 18;56(6):763-76. doi: 10.1016/j.molcel.2014.10.015. Epub 2014 Nov 20.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Nucleus / genetics
  • Gene Expression
  • Gene Expression Regulation, Fungal
  • Mitochondria / genetics
  • Multienzyme Complexes
  • Protein Multimerization
  • Proton-Translocating ATPases / genetics*
  • Proton-Translocating ATPases / metabolism
  • RNA-Binding Proteins / physiology
  • Saccharomyces cerevisiae / enzymology
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae Proteins / physiology


  • ARC1 protein, S cerevisiae
  • Multienzyme Complexes
  • RNA-Binding Proteins
  • Saccharomyces cerevisiae Proteins
  • Proton-Translocating ATPases