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Structures of the human mitochondrial ribosome bound to EF-G1 reveal distinct features of mitochondrial translation elongation

Author

Listed:
  • Ravi Kiran Koripella

    (Division of Translational Medicine, Wadsworth Center, New York State Department of Health, Empire State Plaza)

  • Manjuli R. Sharma

    (Division of Translational Medicine, Wadsworth Center, New York State Department of Health, Empire State Plaza)

  • Kalpana Bhargava

    (University of North Carolina
    High Energy Material Research Lab, Defense Research and Development Organization, Sutarwadi, Pashan)

  • Partha P. Datta

    (Division of Translational Medicine, Wadsworth Center, New York State Department of Health, Empire State Plaza
    Department of Biological Sciences, Indian Institute of Science Education and Research Kolkata)

  • Prem S. Kaushal

    (Division of Translational Medicine, Wadsworth Center, New York State Department of Health, Empire State Plaza
    Regional Centre for Biotechnology, 3rd Milestone, Faridabad-Gurgaon Expressway)

  • Pooja Keshavan

    (Division of Translational Medicine, Wadsworth Center, New York State Department of Health, Empire State Plaza)

  • Linda L. Spremulli

    (University of North Carolina)

  • Nilesh K. Banavali

    (Division of Translational Medicine, Wadsworth Center, New York State Department of Health, Empire State Plaza
    Department of Biomedical Sciences, University at Albany, SUNY)

  • Rajendra K. Agrawal

    (Division of Translational Medicine, Wadsworth Center, New York State Department of Health, Empire State Plaza
    Department of Biomedical Sciences, University at Albany, SUNY)

Abstract

The mammalian mitochondrial ribosome (mitoribosome) and its associated translational factors have evolved to accommodate greater participation of proteins in mitochondrial translation. Here we present the 2.68–3.96 Å cryo-EM structures of the human 55S mitoribosome in complex with the human mitochondrial elongation factor G1 (EF-G1mt) in three distinct conformational states, including an intermediate state and a post-translocational state. These structures reveal the role of several mitochondria-specific (mito-specific) mitoribosomal proteins (MRPs) and a mito-specific segment of EF-G1mt in mitochondrial tRNA (tRNAmt) translocation. In particular, the mito-specific C-terminal extension in EF-G1mt is directly involved in translocation of the acceptor arm of the A-site tRNAmt. In addition to the ratchet-like and independent head-swiveling motions exhibited by the small mitoribosomal subunit, we discover significant conformational changes in MRP mL45 at the nascent polypeptide-exit site within the large mitoribosomal subunit that could be critical for tethering of the elongating mitoribosome onto the inner-mitochondrial membrane.

Suggested Citation

  • Ravi Kiran Koripella & Manjuli R. Sharma & Kalpana Bhargava & Partha P. Datta & Prem S. Kaushal & Pooja Keshavan & Linda L. Spremulli & Nilesh K. Banavali & Rajendra K. Agrawal, 2020. "Structures of the human mitochondrial ribosome bound to EF-G1 reveal distinct features of mitochondrial translation elongation," Nature Communications, Nature, vol. 11(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-17715-2
    DOI: 10.1038/s41467-020-17715-2
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    Cited by:

    1. Thu Giang Nguyen & Christina Ritter & Eva Kummer, 2023. "Structural insights into the role of GTPBP10 in the RNA maturation of the mitoribosome," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    2. Vivek Singh & Yuzuru Itoh & Samuel Del’Olio & Asem Hassan & Andreas Naschberger & Rasmus Kock Flygaard & Yuko Nobe & Keiichi Izumikawa & Shintaro Aibara & Juni Andréll & Paul C. Whitford & Antoni Barr, 2024. "Mitoribosome structure with cofactors and modifications reveals mechanism of ligand binding and interactions with L1 stalk," Nature Communications, Nature, vol. 15(1), pages 1-22, December.

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