ArticleNucleic acids research2021
Human GTPBP5 is involved in the late stage of mitoribosome large subunit assembly.
Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 32 citations in OpenAlex.
- Role of mitochondrial translation in modulating inflammatory disease outcome: Current knowledge and future perspectives.The Journal of biological chemistry · 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
- The DEAD-box RNA helicase DDX28 suppresses cell migration and 3D growth and invasion in MDA-MB-231 cells by altering bioenergetics.Molecular biology of the cell · 2025Article
- The mitochondrial methylation potential gates mitoribosome assembly.Nature communications · 2025Article
- WBSCR16 is essential for mitochondrial 16S rRNA processing in mammals.Nucleic acids research · 2025Article
- The role of m5C, m1A and m7G modifications in tumors of urinary system.Frontiers in cell and developmental biology · 2025Review
- GTPBP8 plays a role in mitoribosome formation in human mitochondria.Nature communications · 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
- Transcriptomic Networks Reveal the Tissue-Specific Cold Shock Responses in Japanese Flounder (Biology · 2023Article
- Primary and metastatic tumors exhibit systems-level differences in dependence on mitochondrial respiratory function.PLoS biology · 2022Article
- The structure-function analysis of Obg-like GTPase proteins along the evolutionary tree from bacteria to humans.Genes to cells : devoted to molecular & cellular mechanisms · 2022Review
- 5-methylcytosine RNA methyltransferases and their potential roles in cancer.Journal of translational medicine · 2022Review
- A late-stage assembly checkpoint of the human mitochondrial ribosome large subunit.Nature communications · 2022Article
- 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
- Structural basis for late maturation steps of the human mitoribosomal large subunit.Nature communications · 2021Article
- Human Mitoribosome Biogenesis and Its Emerging Links to Disease.International journal of molecular sciences · 2021Review
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Authors and funding
11 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human mitoribosomes are macromolecular complexes essential for translation of 11 mitochondrial mRNAs. The large and the small mitoribosomal subunits undergo a multistep maturation process that requires the involvement of several factors. Among these factors, GTP-binding proteins (GTPBPs) play an important role as GTP hydrolysis can provide energy throughout the assembly stages. In bacteria, many GTPBPs are needed for the maturation of ribosome subunits and, of particular interest for this study, ObgE has been shown to assist in the 50S subunit assembly. Here, we characterize the role of a related human Obg-family member, GTPBP5. We show that GTPBP5 interacts specifically with the large mitoribosomal subunit (mt-LSU) proteins and several late-stage mitoribosome assembly factors, including MTERF4:NSUN4 complex, MRM2 methyltransferase, MALSU1 and MTG1. Interestingly, we find that interaction of GTPBP5 with the mt-LSU is compromised in the presence of a non-hydrolysable analogue of GTP, implying a different mechanism of action of this protein in contrast to that of other Obg-family GTPBPs. GTPBP5 ablation leads to severe impairment in the oxidative phosphorylation system, concurrent with a decrease in mitochondrial translation and reduced monosome formation. Overall, our data indicate an important role of GTPBP5 in mitochondrial function and suggest its involvement in the late-stage of mt-LSU maturation.
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