Distinct pre-initiation steps in human mitochondrial translation

Anas Khawaja, Yuzuru Itoh, Cristina Remes, Henrik Spåhr, Olessya Yukhnovets, Henning Höfig, Alexey Amunts () and Joanna Rorbach ()
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Anas Khawaja: Division of Molecular Metabolism, Karolinska Institutet, Biomedicum
Yuzuru Itoh: Division of Molecular Metabolism, Karolinska Institutet, Biomedicum
Cristina Remes: Max-Planck-Institute for Biology of Ageing
Henrik Spåhr: Division of Molecular Metabolism, Karolinska Institutet, Biomedicum
Olessya Yukhnovets: RWTH Aachen, I. Physikalisches Institut (IA)
Henning Höfig: RWTH Aachen, I. Physikalisches Institut (IA)
Alexey Amunts: Division of Molecular Metabolism, Karolinska Institutet, Biomedicum
Joanna Rorbach: Division of Molecular Metabolism, Karolinska Institutet, Biomedicum

Nature Communications, 2020, vol. 11, issue 1, 1-10

Abstract: Abstract 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 mammalian protein synthesis that are specific to mitochondria.

Date: 2020
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DOI: 10.1038/s41467-020-16503-2

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