Journal Article

FZJ-2020-02621

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Distinct pre-initiation steps in human mitochondrial translation

Khawaja, A. ; Itoh, Y. ; Remes, C. ; Spåhr, H. ; Yukhnovets, O.FZJ* ; Höfig, H. ; Amunts, A. (Corresponding author) ; Rorbach, J. (Corresponding author)

2020
Nature Publishing Group UK [London]

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Please use a persistent id in citations: http://hdl.handle.net/2128/25332  doi:10.1038/s41467-020-16503-2

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 mammal

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Contributing Institute(s):

1. Zelluläre Strukturbiologie (IBI-6)

Research Program(s):

1. 551 - Functional Macromolecules and Complexes (POF3-551) (POF3-551)

Appears in the scientific report 2020

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