ArticleNucleic acids research2020
Human GTPBP5 (MTG2) fuels mitoribosome large subunit maturation by facilitating 16S rRNA methylation.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 49 citations in OpenAlex.
- Regulation of RNA-binding proteins by small biomolecules.Nature reviews. Molecular cell biology · 2026Review
- MTG2 as a Causal and Druggable Target in Uveal Melanoma via Mitochondrial DNA Dynamics: Evidence From Functional Validation and DMSA Identification.Investigative ophthalmology & visual science · 2026Article
- A five-gene mitochondria-associated prognostic signature for bladder cancer.International journal of clinical and experimental pathology · 2026Article
- The late stages of yeast mitoribosome large subunit biogenesis.Biochimica et biophysica acta. Molecular cell research · 2025Article
- WBSCR16 is essential for mitochondrial 16S rRNA processing in mammals.Nucleic acids research · 2025Article
- Mitochondrial ribosome biogenesis and redox sensing.FEBS open bio · 2024Review
- GTPBP8 plays a role in mitoribosome formation in human mitochondria.Nature communications · 2024Article
- GTPBP8 modulates mitochondrial fission through a Drp1-dependent process.Journal of cell science · 2024Article
- The zinc finger motif in the mitochondrial large ribosomal subunit protein bL36m is essential for optimal yeast mitoribosome assembly and function.Biochimica et biophysica acta. Molecular cell research · 2024Article
- Molecular pathways in mitochondrial disorders due to a defective mitochondrial protein synthesis.Frontiers in cell and developmental biology · 2024Review
- Structural insights into the role of GTPBP10 in the RNA maturation of the mitoribosome.Nature communications · 2023Article
- GTPBP8 is required for mitoribosomal biogenesis and mitochondrial translation.Cellular and molecular life sciences : CMLS · 2023Article
- Metabolic Labeling of Mitochondrial Translation Products in Whole Cells and Isolated Organelles.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Mitoribosome Biogenesis.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Transcriptomic and proteomic retinal pigment epithelium signatures of age-related macular degeneration.Nature communications · 2022Article
- Functional analyses of mitoribosome 54S subunit devoid of mitochondria-specific protein sequences.Yeast (Chichester, England) · 2022Article
- A late-stage assembly checkpoint of the human mitochondrial ribosome large subunit.Nature communications · 2022Article
- Entropy-Based Graph Clustering of PPI Networks for Predicting Overlapping Functional Modules of Proteins.Entropy (Basel, Switzerland) · 2021Article
- A distinct assembly pathway of the human 39S late pre-mitoribosome.Nature communications · 2021Article
- Structural basis of GTPase-mediated mitochondrial ribosome biogenesis and recycling.Nature communications · 2021Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Biogenesis of mammalian mitochondrial ribosomes (mitoribosomes) involves several conserved small GTPases. Here, we report that the Obg family protein GTPBP5 or MTG2 is a mitochondrial protein whose absence in a TALEN-induced HEK293T knockout (KO) cell line leads to severely decreased levels of the 55S monosome and attenuated mitochondrial protein synthesis. We show that a fraction of GTPBP5 co-sediments with the large mitoribosome subunit (mtLSU), and crosslinks specifically with the 16S rRNA, and several mtLSU proteins and assembly factors. Notably, the latter group includes MTERF4, involved in monosome assembly, and MRM2, the methyltransferase that catalyzes the modification of the 16S mt-rRNA A-loop U1369 residue. The GTPBP5 interaction with MRM2 was also detected using the proximity-dependent biotinylation (BioID) assay. In GTPBP5-KO mitochondria, the mtLSU lacks bL36m, accumulates an excess of the assembly factors MTG1, GTPBP10, MALSU1 and MTERF4, and contains hypomethylated 16S rRNA. We propose that GTPBP5 primarily fuels proper mtLSU maturation by securing efficient methylation of two 16S rRNA residues, and ultimately serves to coordinate subunit joining through the release of late-stage mtLSU assembly factors. In this way, GTPBP5 provides an ultimate quality control checkpoint function during mtLSU assembly that minimizes premature subunit joining to ensure the assembly of the mature 55S monosome.
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