Interconnected assembly factors regulate the biogenesis of mitoribosomal large subunit

• DOI: 10.15252/embj.2020106292
• Publication Date: 2021-02-14T11:28:20Z
• Authors: Victor Tobiasson; Ondřej Gahura; Shintaro Aibara; Rozbeh Baradaran; Alena Zíková; Alexey Amunts
• Keywords: Ribosomal protein

Mitoribosomes consist of ribosomal RNA and protein components, coordinated assembly which is critical for function. We used mitoribosomes from Trypanosoma brucei with reduced increased mass to provide insights into the biogenesis mitoribosomal large subunit. Structural characterization a stable intermediate revealed 22 factors, some have orthologues/counterparts/homologues in mammalian genomes. These factors form network that spans distance 180 Å, shielding surface. The central protuberance L7/L12 stalk are not assembled entirely require removal remodeling proteins become functional. conserved GTPBP7 mt-EngA bound together at subunit interface proximity peptidyl transferase center. A mitochondrial acyl-carrier plays role docking L1 stalk, needs be repositioned during maturation. Additional enzymatically deactivated scaffold while exit tunnel blocked. Together, this extensive accessory stabilizes immature sites connects functionally important regions