ArticleNucleic acids research2023
Cleavage kinetics of human mitochondrial RNase P and contribution of its non-nuclease subunits.
Article in Nucleic acids research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 20 citations in OpenAlex.
- Targeting NSignal transduction and targeted therapy · 2026Article
- Pathogenic human mitochondrial tRNA variants impair RNA processing by compromising 5' leader removal.bioRxiv : the preprint server for biology · 2026Article
- Tangled but ordered human mitochondrial tRNA maturation.Science China. Life sciences · 2025Article
- Substrate and enzyme determinants for recognition by human mitochondrial RNase P.Nucleic acids research · 2025Article
- FASTKD5 processes mitochondrial pre-mRNAs at noncanonical cleavage sites.Nucleic acids research · 2025Article
- Molecular basis of human nuclear and mitochondrial tRNA 3' processing.Nature structural & molecular biology · 2025Article
- Structural basis of 3'-tRNA maturation by the human mitochondrial RNase Z complex.The EMBO journal · 2024Article
- Structural insights into human ELAC2 as a tRNA 3' processing enzyme.Nucleic acids research · 2024Article
- Post-transcriptional methylation of mitochondrial-tRNA differentially contributes to mitochondrial pathology.Nature communications · 2024Article
- TRMT10C-mediated m7G modification of circFAM126A inhibits lung cancer growth by regulating cellular glycolysis.Cell biology and toxicology · 2024Article
- RNA modifying enzymes shape tRNA biogenesis and function.The Journal of biological chemistry · 2024Review
- Mitochondrial Genome-Encoded Long Noncoding RNABiomedicines · 2024Article
- The making and breaking of tRNAs by ribonucleases.Trends in genetics : TIG · 2024Review
- Structural basis for human mitochondrial tRNA maturation.Nature communications · 2024Article
- Discovery, structure, mechanisms, and evolution of protein-only RNase P enzymes.The Journal of biological chemistry · 2024Review
- The protein-only RNase Ps, endonucleases that cleave pre-tRNA: Biological relevance, molecular architectures, substrate recognition and specificity, and protein interactomes.Wiley interdisciplinary reviews. RNAArticle
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RNase P is the endonuclease responsible for the 5' processing of precursor tRNAs (pre-tRNAs). Unlike the single-subunit protein-only RNase P (PRORP) found in plants or protists, human mitochondrial RNase P is a multi-enzyme assembly that in addition to the homologous PRORP subunit comprises a methyltransferase (TRMT10C) and a dehydrogenase (SDR5C1) subunit; these proteins, but not their enzymatic activities, are required for efficient pre-tRNA cleavage. Here we report a kinetic analysis of the cleavage reaction by human PRORP and its interplay with TRMT10C-SDR5C1 including 12 different mitochondrial pre-tRNAs. Surprisingly, we found that PRORP alone binds pre-tRNAs with nanomolar affinity and can even cleave some of them at reduced efficiency without the other subunits. Thus, the ancient binding mode, involving the tRNA elbow and PRORP's PPR domain, appears basically retained by human PRORP, and its metallonuclease domain is in principle correctly folded and functional. Our findings support a model according to which the main function of TRMT10C-SDR5C1 is to direct PRORP's nuclease domain to the cleavage site, thereby increasing the rate and accuracy of cleavage. This functional dependence of human PRORP on an extra tRNA-binding protein complex likely reflects an evolutionary adaptation to the erosion of canonical structural features in mitochondrial tRNAs.
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