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 () and Nenad Ban ()
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Basil J. Greber: Institute of Molecular Biology and Biophysics, Schafmattstrasse 20, ETH Zurich, CH-8093 Zurich, Switzerland
Daniel Boehringer: Institute of Molecular Biology and Biophysics, Schafmattstrasse 20, ETH Zurich, CH-8093 Zurich, Switzerland
Alexander Leitner: Institute of Molecular Systems Biology, Wolfgang-Pauli-Strasse 16, ETH Zurich, CH-8093 Zurich, Switzerland
Philipp Bieri: Institute of Molecular Biology and Biophysics, Schafmattstrasse 20, ETH Zurich, CH-8093 Zurich, Switzerland
Felix Voigts-Hoffmann: Institute of Molecular Biology and Biophysics, Schafmattstrasse 20, ETH Zurich, CH-8093 Zurich, Switzerland
Jan P. Erzberger: Institute of Molecular Biology and Biophysics, Schafmattstrasse 20, ETH Zurich, CH-8093 Zurich, Switzerland
Marc Leibundgut: Institute of Molecular Biology and Biophysics, Schafmattstrasse 20, ETH Zurich, CH-8093 Zurich, Switzerland
Ruedi Aebersold: Institute of Molecular Systems Biology, Wolfgang-Pauli-Strasse 16, ETH Zurich, CH-8093 Zurich, Switzerland
Nenad Ban: Institute of Molecular Biology and Biophysics, Schafmattstrasse 20, ETH Zurich, CH-8093 Zurich, Switzerland

Nature, 2014, vol. 505, issue 7484, 515-519

Abstract: Abstract 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.

Date: 2014
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DOI: 10.1038/nature12890

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