A heme-sensing mechanism in the translational regulation of mitochondrial cytochrome c oxidase biogenesis

Iliana C. Soto, Flavia Fontanesi, Richard S. Myers, Patrice Hamel, Antoni Barrientos

Research output: Contribution to journalArticle

47 Scopus citations

Abstract

Heme plays fundamental roles as cofactor and signaling molecule in multiple pathways devoted to oxygen sensing and utilization in aerobic organisms. For cellular respiration, heme serves as a prosthetic group in electron transfer proteins and redox enzymes. Here we report that in the yeast Saccharomyces cerevisiae, a heme-sensing mechanism translationally controls the biogenesis of cytochrome c oxidase (COX), the terminal mitochondrial respiratory chain enzyme. We show that Mss51, a COX1 mRNA-specific translational activator and Cox1 chaperone, which coordinates Cox1 synthesis in mitoribosomes with its assembly in COX, is a heme-binding protein. Mss51 contains two heme regulatory motifs or Cys-Pro-X domains located in its N terminus. Using a combination of in vitro and in vivo approaches, we have demonstrated that these motifs are important for heme binding and efficient performance of Mss51 functions. We conclude that heme sensing by Mss51 regulates COX biogenesis and aerobic energy production.

Original languageEnglish (US)
Pages (from-to)801-813
Number of pages13
JournalCell Metabolism
Volume16
Issue number6
DOIs
StatePublished - Dec 5 2012

ASJC Scopus subject areas

  • Physiology
  • Molecular Biology
  • Cell Biology

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