ArticleNature structural & molecular biology2024
A roadmap for ribosome assembly in human mitochondria.
Article in Nature structural & molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Pseudouridine synthase PUS1 and initiation factor mtIF2 are human mitoribosomal small subunit assembly factors.Nature communications · 2026Article
- MRPS22 variants alter mitochondrial ribosome assembly in patients with leukodystrophy, movement disorder and intellectual impairment.Human molecular genetics · 2026Article
- Mitochondrial translational control in cardiovascular diseases: from mechanisms to therapies.Redox biology · 2026Review
- A biallelic MRPL42 variant causes a combined oxidative phosphorylation deficiency syndrome revealed by multi-omics.NPJ genomic medicine · 2026Article
- Structural remodeling of the mitochondrial protein biogenesis machinery under proteostatic stress.Science advances · 2026Article
- RiboBright reveals cell-type-specific differences in ribosome organization and movement.Nature communications · 2026Article
- Spatiotemporal control of mitoribosome-mediated metabolic reprogramming in cancer: implications for heterogeneity and therapeutic targeting.Frontiers in cell and developmental biology · 2026Review
- Structural insights into cauliflower mitoribosome in translation state and in association with a late assembly factor.Nature communications · 2025Article
- The late stages of yeast mitoribosome large subunit biogenesis.Biochimica et biophysica acta. Molecular cell research · 2025Article
- Mettl15-Mettl17 modulates the transition from early to late pre-mitoribosome.Structure (London, England : 1993) · 2025Article
- Functionally dominant hotspot mutations of mitochondrial ribosomal RNA genes in cancer.Nature genetics · 2025Article
- The mitochondrial methylation potential gates mitoribosome assembly.Nature communications · 2025Article
- Ubiquitin-Proteasome System Dysregulation in Alzheimer's Disease Impacts Protein Abundance.bioRxiv : the preprint server for biology · 2025Article
- Spatial analysis of mitochondrial gene expression reveals dynamic translation hubs and remodeling in stress.Science advances · 2025Article
- Coupling of ribosome biogenesis and translation initiation in human mitochondria.Nature communications · 2025Article
- The Origin of Life in the Early Continental Crust: A Comprehensive Model.Life (Basel, Switzerland) · 2025Article
- A spatial atlas of mitochondrial gene expression reveals dynamic translation hubs and remodeling in stress.bioRxiv : the preprint server for biology · 2024Article
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15 authors.
Funding
Abstract
Mitochondria contain dedicated ribosomes (mitoribosomes), which synthesize the mitochondrial-encoded core components of the oxidative phosphorylation complexes. The RNA and protein components of mitoribosomes are encoded on two different genomes (mitochondrial and nuclear) and are assembled into functional complexes with the help of dedicated factors inside the organelle. Defects in mitoribosome biogenesis are associated with severe human diseases, yet the molecular pathway of mitoribosome assembly remains poorly understood. Here, we applied a multidisciplinary approach combining biochemical isolation and analysis of native mitoribosomal assembly complexes with quantitative mass spectrometry and mathematical modeling to reconstitute the entire assembly pathway of the human mitoribosome. We show that, in contrast to its bacterial and cytosolic counterparts, human mitoribosome biogenesis involves the formation of ribosomal protein-only modules, which then assemble on the appropriate ribosomal RNA moiety in a coordinated fashion. The presence of excess protein-only modules primed for assembly rationalizes how mitochondria cope with the challenge of forming a protein-rich ribonucleoprotein complex of dual genetic origin. This study provides a comprehensive roadmap of mitoribosome biogenesis, from very early to late maturation steps, and highlights the evolutionary divergence from its bacterial ancestor.
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