CLPP coordinates mitoribosomal assembly through the regulation of ERAL1 levels

Karolina Szczepanowska, Priyanka Maiti, Alexandra Kukat, Eduard Hofsetz, Hendrik Nolte, Katharina Senft, Christina Becker, Benedetta Ruzzenente, Hue Tran Hornig-Do, Rolf Wibom, Rudolf J. Wiesner, Marcus Krüger, Aleksandra Trifunovic

Research output: Contribution to journalArticlepeer-review

81 Scopus citations


Despite being one of the most studied proteases in bacteria, very little is known about the role of ClpXP in mitochondria. We now present evidence that mammalian CLPP has an essential role in determining the rate of mitochondrial protein synthesis by regulating the level of mitoribosome assembly. Through a proteomic approach and the use of a catalytically inactive CLPP, we produced the first comprehensive list of possible mammalian ClpXP substrates involved in the regulation of mitochondrial translation, oxidative phosphorylation, and a number of metabolic pathways. We further show that the defect in mitoribosomal assembly is a consequence of the accumulation of ERAL1, a putative 12S rRNA chaperone, and novel ClpXP substrate. The presented data suggest that the timely removal of ERAL1 from the small ribosomal subunit is essential for the efficient maturation of the mitoribosome and a normal rate of mitochondrial translation.

Original languageEnglish (US)
Pages (from-to)2566-2583
Number of pages18
JournalEMBO Journal
Issue number23
StatePublished - Dec 1 2016
Externally publishedYes


  • CLPP
  • ERAL1
  • mitochondrial ribosome assembly
  • OXPHOS deficiency

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)


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