Structures of the human mitochondrial ribosome bound to EF-G1 reveal distinct features of mitochondrial translation elongation
Copyright policy )Structures of the human mitochondrial ribosome bound to EF-G1 reveal distinct features of mitochondrial translation elongation
AbstractThe 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.
- New York State Department of Health United States
- Indian Institute of Science Education and Research Kolkata India
- University of North Carolina at Greensboro United States
- University of North Carolina at Chapel Hill United States
- State University of New York at Potsdam United States
Models, Molecular, Protein Conformation, alpha-Helical, Ribosomal Proteins, RNA, Mitochondrial, Science, Peptide Chain Elongation, Translational, Article, Mitochondrial Proteins, RNA, Transfer, Humans, Protein Interaction Domains and Motifs, Amino Acid Sequence, Binding Sites, Q, Cryoelectron Microscopy, Peptide Elongation Factor G, Recombinant Proteins, Mitochondria, HEK293 Cells, Mitochondrial Membranes, Nucleic Acid Conformation, Protein Conformation, beta-Strand, Protein Binding
Models, Molecular, Protein Conformation, alpha-Helical, Ribosomal Proteins, RNA, Mitochondrial, Science, Peptide Chain Elongation, Translational, Article, Mitochondrial Proteins, RNA, Transfer, Humans, Protein Interaction Domains and Motifs, Amino Acid Sequence, Binding Sites, Q, Cryoelectron Microscopy, Peptide Elongation Factor G, Recombinant Proteins, Mitochondria, HEK293 Cells, Mitochondrial Membranes, Nucleic Acid Conformation, Protein Conformation, beta-Strand, Protein Binding
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