Abstract
Final maturation steps during ribosome biogenesis require the assistance of assembly and quality control factors to ensure the folding of rRNA and proteins into a functional translation machinery. Here we integrate several recent structural snapshots of native large ribosomal subunit intermediates into the complex pathway of mitochondrial ribosome assembly.
Highlights
Final maturation steps during ribosome biogenesis require the assistance of assembly and quality control factors to ensure the folding of rRNA and proteins into a functional translation machinery
Several structural snapshots of intermediate states of large ribosomal subunit (LSU) assembly isolated from human and protist mitochondria as well as from bacteria have been reported. This was achieved by applying genetic perturbation or affinity purification of ribosome biogenesis factors followed by cryo-electron microscopy
These structures reveal the molecular function and hierarchical order of action for several essential assembly factors. We integrate these recent studies into a stepwise model of mitochondrial LSU biogenesis, which highlights similarities to its bacterial counterpart and organelle-specific features
Summary
Final maturation steps during ribosome biogenesis require the assistance of assembly and quality control factors to ensure the folding of rRNA and proteins into a functional translation machinery. It has the mitochondrial assembly of ribosomal large subunit protein 1 (MALSU1) module, the RNA helicase DDX28, the GTPase GTPBP10 and a dimer of the 2′-O-methyltransferase MRM3 bound. MALSU1 associates with L0R8F8 and mitochondrial acyl carrier protein (mtACP) to form an antiassociation module that interacts with uL14m, bL19m, and the sarcin-ricin loop (SRL, h95) to obstruct subunit joining [2].
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