Mechanism of mitoribosomal small subunit biogenesis and preinitiation

Yuzuru Itoh, Anas Khawaja, Ivan Laptev, Miriam Cipullo, Ilian Atanassov, Petr Sergiev, Joanna Rorbach () and Alexey Amunts ()
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Yuzuru Itoh: Stockholm University
Anas Khawaja: Karolinska Institute
Ivan Laptev: Center of Life Sciences, Skolkovo Institute of Science and Technology
Miriam Cipullo: Karolinska Institute
Ilian Atanassov: Proteomics Core Facility, Max-Planck-Institute for Biology of Ageing
Petr Sergiev: Center of Life Sciences, Skolkovo Institute of Science and Technology
Joanna Rorbach: Karolinska Institute
Alexey Amunts: Stockholm University

Nature, 2022, vol. 606, issue 7914, 603-608

Abstract: Abstract Mitoribosomes are essential for the synthesis and maintenance of bioenergetic proteins. Here we use cryo-electron microscopy to determine a series of the small mitoribosomal subunit (SSU) intermediates in complex with auxiliary factors, revealing a sequential assembly mechanism. The methyltransferase TFB1M binds to partially unfolded rRNA h45 that is promoted by RBFA, while the mRNA channel is blocked. This enables binding of METTL15 that promotes further rRNA maturation and a large conformational change of RBFA. The new conformation allows initiation factor mtIF3 to already occupy the subunit interface during the assembly. Finally, the mitochondria-specific ribosomal protein mS37 (ref. 1) outcompetes RBFA to complete the assembly with the SSU–mS37–mtIF3 complex2 that proceeds towards mtIF2 binding and translation initiation. Our results explain how the action of step-specific factors modulate the dynamic assembly of the SSU, and adaptation of a unique protein, mS37, links the assembly to initiation to establish the catalytic human mitoribosome.

Date: 2022
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DOI: 10.1038/s41586-022-04795-x

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