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

Ravi Kiran Koripella, Manjuli R. Sharma, Kalpana Bhargava, Partha P. Datta, Prem S. Kaushal, Pooja Keshavan, Linda L. Spremulli, Nilesh K. Banavali and Rajendra K. Agrawal ()
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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
Partha P. Datta: Division of Translational Medicine, Wadsworth Center, New York State Department of Health, Empire State Plaza
Prem S. Kaushal: Division of Translational Medicine, Wadsworth Center, New York State Department of Health, Empire State Plaza
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
Rajendra K. Agrawal: Division of Translational Medicine, Wadsworth Center, New York State Department of Health, Empire State Plaza

Nature Communications, 2020, vol. 11, issue 1, 1-11

Abstract: 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.

Date: 2020
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DOI: 10.1038/s41467-020-17715-2

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