| Home > Publications database > Distinct pre-initiation steps in human mitochondrial translation > print |
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| 024 | 7 | _ | |a 10.1038/s41467-020-16503-2 |2 doi |
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| 100 | 1 | _ | |a Khawaja, Anas |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Distinct pre-initiation steps in human mitochondrial translation |
| 260 | _ | _ | |a [London] |c 2020 |b Nature Publishing Group UK |
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| 520 | _ | _ | |a Translation initiation in human mitochondria relies upon specialized mitoribosomes and initiation factors, mtIF2 and mtIF3, which have diverged from their bacterial counterparts. Here we report two distinct mitochondrial pre-initiation assembly steps involving those factors. Single-particle cryo-EM revealed that in the first step, interactions between mitochondria-specific protein mS37 and mtIF3 keep the small mitoribosomal subunit in a conformation favorable for a subsequent accommodation of mtIF2 in the second step. Combination with fluorescence cross-correlation spectroscopy analyses suggests that mtIF3 promotes complex assembly without mRNA or initiator tRNA binding, where exclusion is achieved by the N-terminal and C-terminal domains of mtIF3. Finally, the association of large mitoribosomal subunit is required for initiator tRNA and leaderless mRNA recruitment to form a stable initiation complex. These data reveal fundamental aspects of mammal |
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| 700 | 1 | _ | |a Itoh, Yuzuru |0 0000-0001-7802-5572 |b 1 |
| 700 | 1 | _ | |a Remes, Cristina |0 P:(DE-Juel1)156351 |b 2 |
| 700 | 1 | _ | |a Spåhr, Henrik |0 P:(DE-HGF)0 |b 3 |
| 700 | 1 | _ | |a Yukhnovets, Olessya |0 P:(DE-Juel1)176889 |b 4 |
| 700 | 1 | _ | |a Höfig, Henning |0 P:(DE-Juel1)165927 |b 5 |
| 700 | 1 | _ | |a Amunts, Alexey |0 0000-0002-5302-1740 |b 6 |e Corresponding author |
| 700 | 1 | _ | |a Rorbach, Joanna |0 0000-0002-2891-2840 |b 7 |e Corresponding author |
| 773 | _ | _ | |a 10.1038/s41467-020-16503-2 |g Vol. 11, no. 1, p. 2932 |0 PERI:(DE-600)2553671-0 |n 1 |p 2932 |t Nature Communications |v 11 |y 2020 |x 2041-1723 |
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