ArticleProceedings of the National Academy of Sciences of the United States of America2012
Mitochondrial ribonuclease P structure provides insight into the evolution of catalytic strategies for precursor-tRNA 5' processing.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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Who cites it
73 citing papers in PubMed, 115 citations in OpenAlex.
- Structural basis for protein-free catalysis by ribonuclease P ribozyme.Nature communications · 2026Article
- Structures of pentatricopeptide repeat proteins.Acta crystallographica. Section F, Structural biology communications · 2026Review
- Composite SMG5-SMG6 PIN domain formation is essential for NMD.Nature communications · 2026Article
- Substrate and enzyme determinants for recognition by human mitochondrial RNase P.Nucleic acids research · 2025Article
- Structural basis of transfer RNA processing by bacterial minimal RNase P.Nature communications · 2025Article
- Structural basis for human mitochondrial tRNA maturation.Nature communications · 2024Article
- Applications of Synthetic Pentatricopeptide Repeat Proteins.Plant & cell physiology · 2024Review
- Discovery, structure, mechanisms, and evolution of protein-only RNase P enzymes.The Journal of biological chemistry · 2024Review
- Recognition of the tRNA structure: Everything everywhere but not all at once.Cell chemical biology · 2024Review
- A tRNA-modifying enzyme facilitates RNase P activity in Arabidopsis nuclei.Nature plants · 2023Article
- Cleavage kinetics of human mitochondrial RNase P and contribution of its non-nuclease subunits.Nucleic acids research · 2023Article
- Importance of residue 248 in Escherichia coli RNase P RNA mediated cleavage.Scientific reports · 2023Article
- How RNases Shape Mitochondrial Transcriptomes.International journal of molecular sciences · 2022Review
- Crystal structures and insights into precursor tRNA 5'-end processing by prokaryotic minimal protein-only RNase P.Nature communications · 2022Article
- Not making the cut: Techniques to prevent RNA cleavage in structural studies of RNase-RNA complexes.Journal of structural biology: X · 2022Review
- Positively selected genes in the hoary bat (PeerJ · 2022Article
- Cooperativity and Interdependency between RNA Structure and RNA-RNA Interactions.Non-coding RNA · 2021Review
- Bi-allelic variants in the mitochondrial RNase P subunit PRORP cause mitochondrial tRNA processing defects and pleiotropic multisystem presentations.American journal of human genetics · 2021Article
- Post-transcriptional diversity in riboproteins and RNAs in aging and cancer.Seminars in cancer biology · 2021Review
- The Dynamic Network of RNP RNase P Subunits.International journal of molecular sciences · 2021Review
13 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Ribonuclease P (RNase P) catalyzes the maturation of the 5' end of tRNA precursors. Typically these enzymes are ribonucleoproteins with a conserved RNA component responsible for catalysis. However, protein-only RNase P (PRORP) enzymes process precursor tRNAs in human mitochondria and in all tRNA-using compartments of Arabidopsis thaliana. PRORP enzymes are nuclear encoded and conserved among many eukaryotes, having evolved recently as yeast mitochondrial genomes encode an RNase P RNA. Here we report the crystal structure of PRORP1 from A. thaliana at 1.75 Å resolution, revealing a prototypical metallonuclease domain tethered to a pentatricopeptide repeat (PPR) domain by a structural zinc-binding domain. The metallonuclease domain is a unique high-resolution structure of a Nedd4-BP1, YacP Nucleases (NYN) domain that is a member of the PIN domain-like fold superfamily, including the FLAP nuclease family. The structural similarity between PRORP1 and the FLAP nuclease family suggests that they evolved from a common ancestor. Biochemical data reveal that conserved aspartate residues in PRORP1 are important for catalytic activity and metal binding and that the PPR domain also enhances activity, likely through an interaction with pre-tRNA. These results provide a foundation for understanding tRNA maturation in organelles. Furthermore, these studies allow for a molecular-level comparison of the catalytic strategies used by the only known naturally evolved protein and RNA-based catalysts that perform the same biological function, pre-tRNA maturation, thereby providing insight into the differences between the prebiotic RNA world and the present protein-dominated world.
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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.