ArticleNature communications2021
Structural basis for late maturation steps of the human mitoribosomal large subunit.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 55 citations in OpenAlex.
- Peroxisomal Import Stress Drives Cellular Senescence through SCAF1-dependent Suppression of Mitoribosome Biogenesis.bioRxiv : the preprint server for biology · 2026Article
- Review
- Pseudouridine synthase PUS1 and initiation factor mtIF2 are human mitoribosomal small subunit assembly factors.Nature communications · 2026Article
- Mechanisms and disease relevance of mitochondrial translation in humans.Nature reviews. Molecular cell biology · 2026Review
- Mechanistic insights into E. coli recovery from growth arrest.Nature communications · 2026Article
- Structural basis of TACO1-mediated efficient mitochondrial translation.Nature communications · 2026Article
- Mechanistic insights intobioRxiv : the preprint server for biology · 2026Article
- Spatiotemporal control of mitoribosome-mediated metabolic reprogramming in cancer: implications for heterogeneity and therapeutic targeting.Frontiers in cell and developmental biology · 2026Review
- Structural Basis of TACO1-Mediated Efficient Mitochondrial Translation.bioRxiv : the preprint server for biology · 2025Article
- 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
- A comprehensive tRNA pseudouridine map uncovers targets dependent on human stand-alone pseudouridine synthases.Nature cell biology · 2025Article
- Targeting tRNA methyltransferases: from molecular mechanisms to drug discovery.Science China. Life sciences · 2025Review
- The mitochondrial methylation potential gates mitoribosome assembly.Nature communications · 2025Article
- Structural insight into the novel Thermus thermophilus SPOUT methyltransferase RlmR catalysing Um2552 formation in the 23S rRNA A-loop: a case of convergent evolution.Nucleic acids research · 2025Article
- Coupling of ribosome biogenesis and translation initiation in human mitochondria.Nature communications · 2025Article
- HflX-mediated drug resistance through ribosome splitting and rRNA disordering in mycobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A roadmap for ribosome assembly in human mitochondria.Nature structural & molecular biology · 2024Article
- Mitochondrial ribosome biogenesis and redox sensing.FEBS open bio · 2024Review
- GTPBP8 plays a role in mitoribosome formation in human mitochondria.Nature communications · 2024Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mitochondrial ribosomes (mitoribosomes) synthesize a critical set of proteins essential for oxidative phosphorylation. Therefore, mitoribosomal function is vital to the cellular energy supply. Mitoribosome biogenesis follows distinct molecular pathways that remain poorly understood. Here, we determine the cryo-EM structures of mitoribosomes isolated from human cell lines with either depleted or overexpressed mitoribosome assembly factor GTPBP5, allowing us to capture consecutive steps during mitoribosomal large subunit (mt-LSU) biogenesis. Our structures provide essential insights into the last steps of 16S rRNA folding, methylation and peptidyl transferase centre (PTC) completion, which require the coordinated action of nine assembly factors. We show that mammalian-specific MTERF4 contributes to the folding of 16S rRNA, allowing 16 S rRNA methylation by MRM2, while GTPBP5 and NSUN4 promote fine-tuning rRNA rearrangements leading to PTC formation. Moreover, our data reveal an unexpected involvement of the elongation factor mtEF-Tu in mt-LSU assembly, where mtEF-Tu interacts with GTPBP5, similar to its interaction with tRNA during translational elongation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.