Architecture of the large subunit of the mammalian mitochondrial ribosome

Basil J. Greber, Daniel Boehringer, Alexander Leitner, Philipp Bieri, Felix Voigts-Hoffmann, Jan P. Erzberger, Marc Leibundgut, Ruedi Aebersold, Nenad Ban

Research output: Contribution to journalArticlepeer-review

166 Scopus citations


Mitochondrial ribosomes synthesize a number of highly hydrophobic proteins encoded on the genome of mitochondria, the organelles in eukaryotic cells that are responsible for energy conversion by oxidative phosphorylation. The ribosomes in mammalian mitochondria have undergone massive structural changes throughout their evolution, including ribosomal RNA shortening and acquisition of mitochondria-specific ribosomal proteins. Here we present the three-dimensional structure of the 39S large subunit of the porcine mitochondrial ribosome determined by cryo-electron microscopy at 4.9 Å resolution. The structure, combined with data from chemical crosslinking and mass spectrometry experiments, reveals the unique features of the 39S subunit at near-atomic resolution and provides detailed insight into the architecture of the polypeptide exit site. This region of the mitochondrial ribosome has been considerably remodelled compared to its bacterial counterpart, providing a specialized platform for the synthesis and membrane insertion of the highly hydrophobic protein components of the respiratory chain.

Original languageEnglish (US)
Pages (from-to)515-519
Number of pages5
Issue number7484
StatePublished - 2014

ASJC Scopus subject areas

  • General


Dive into the research topics of 'Architecture of the large subunit of the mammalian mitochondrial ribosome'. Together they form a unique fingerprint.

Cite this