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A roadmap for ribosome assembly in human mitochondria.

Author information

Affiliations

  • 1. Department of Molecular Biology, University Medical Center Göttingen, Göttingen, Germany.
      Authors
    • Lavdovskaia E 1, 2, 5
    • Challa V 1, 2
    • Heinrichs M 1, 2
    • Richter-Dennerlein R 1, 2, 5
    (4 authors)
  • 2. Department of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany.
      Authors
    • Lavdovskaia E 1, 2, 5
    • Hanitsch E 2
    • Challa V 1, 2
    • Nadler F 2
    • Steube E 2
    • Heinrichs M 1, 2
    • Mai MM 2
    • Richter-Dennerlein R 1, 2, 5
    (8 authors)
  • 3. Bioanalytical Mass Spectrometry Group, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.
      Authors
    • Linden A 3
    • Welp L 3
    • Urlaub H 3, 5
    (3 authors)
  • 4. Quantitative and Systems Biology Group, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.
      Authors
    • Pašen M 4
    • Horokhovskyi Y 4
    • Roetschke HP 4
    • Liepe J 4
    (4 authors)
  • 5. Cluster of Excellence 'Multiscale Bioimaging: from Molecular Machines to Networks of Excitable Cells' (MBExC), University of Göttingen, Göttingen, Germany.
      Authors
    • Lavdovskaia E 1, 2, 5
    • Urlaub H 3, 5
    • Richter-Dennerlein R 1, 2, 5
    (3 authors)

ORCIDs linked to this article

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Nature Structural & Molecular Biology, 11 Jul 2024,
https://doi.org/10.1038/s41594-024-01356-w PMID: 38992089 

Abstract 

Mitochondria contain dedicated ribosomes (mitoribosomes), which synthesize the mitochondrial-encoded core components of the oxidative phosphorylation complexes. The RNA and protein components of mitoribosomes are encoded on two different genomes (mitochondrial and nuclear) and are assembled into functional complexes with the help of dedicated factors inside the organelle. Defects in mitoribosome biogenesis are associated with severe human diseases, yet the molecular pathway of mitoribosome assembly remains poorly understood. Here, we applied a multidisciplinary approach combining biochemical isolation and analysis of native mitoribosomal assembly complexes with quantitative mass spectrometry and mathematical modeling to reconstitute the entire assembly pathway of the human mitoribosome. We show that, in contrast to its bacterial and cytosolic counterparts, human mitoribosome biogenesis involves the formation of ribosomal protein-only modules, which then assemble on the appropriate ribosomal RNA moiety in a coordinated fashion. The presence of excess protein-only modules primed for assembly rationalizes how mitochondria cope with the challenge of forming a protein-rich ribonucleoprotein complex of dual genetic origin. This study provides a comprehensive roadmap of mitoribosome biogenesis, from very early to late maturation steps, and highlights the evolutionary divergence from its bacterial ancestor.

Full text links 

Read article at publisher's site: https://doi.org/10.1038/s41594-024-01356-w

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