ArticleNucleic acids research2020
Pentatricopeptide repeats of protein-only RNase P use a distinct mode to recognize conserved bases and structural elements of pre-tRNA.
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 24 papers.
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Who cites it
24 citing papers in PubMed, 35 citations in OpenAlex.
- Substrate and enzyme determinants for recognition by human mitochondrial RNase P.Nucleic acids research · 2025Article
- Bacterial/archaeal protein-only RNase P: complementation inRNA (New York, N.Y.) · 2025Article
- Article
- Candida albicans PPR proteins are required for the expression of respiratory Complex I subunits.Genetics · 2024Article
- Structural basis of tRNA recognition by the widespread OB fold.Nature communications · 2024Article
- Structural basis for human mitochondrial tRNA maturation.Nature communications · 2024Article
- RNase P: Beyond Precursor tRNA Processing.Genomics, proteomics & bioinformatics · 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
- Targeting FMN, TPP, SAM-I, and glmS Riboswitches with Chimeric Antisense Oligonucleotides for Completely Rational Antibacterial Drug Development.Antibiotics (Basel, Switzerland) · 2023Review
- Cleavage kinetics of human mitochondrial RNase P and contribution of its non-nuclease subunits.Nucleic acids research · 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
- Types and Functions of Mitoribosome-Specific Ribosomal Proteins across Eukaryotes.International journal of molecular sciences · 2022Review
- The many faces of RNA-based RNase P, an RNA-world relic.Trends in biochemical sciences · 2021Review
- The Dynamic Network of RNP RNase P Subunits.International journal of molecular sciences · 2021Review
- A common genetic variant of a mitochondrial RNA processing enzyme predisposes to insulin resistance.Science advances · 2021Article
- Structural basis of RNA processing by human mitochondrial RNase P.Nature structural & molecular biology · 2021Article
- Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Pentatricopeptide repeat (PPR) motifs are α-helical structures known for their modular recognition of single-stranded RNA sequences with each motif in a tandem array binding to a single nucleotide. Protein-only RNase P 1 (PRORP1) in Arabidopsis thaliana is an endoribonuclease that uses its PPR domain to recognize precursor tRNAs (pre-tRNAs) as it catalyzes removal of the 5'-leader sequence from pre-tRNAs with its NYN metallonuclease domain. To gain insight into the mechanism by which PRORP1 recognizes tRNA, we determined a crystal structure of the PPR domain in complex with yeast tRNAPhe at 2.85 Å resolution. The PPR domain of PRORP1 bound to the structurally conserved elbow of tRNA and recognized conserved structural features of tRNAs using mechanisms that are different from the established single-stranded RNA recognition mode of PPR motifs. The PRORP1 PPR domain-tRNAPhe structure revealed a conformational change of the PPR domain upon tRNA binding and moreover demonstrated the need for pronounced overall flexibility in the PRORP1 enzyme conformation for substrate recognition and catalysis. The PRORP1 PPR motifs have evolved strategies for protein-tRNA interaction analogous to tRNA recognition by the RNA component of ribonucleoprotein RNase P and other catalytic RNAs, indicating convergence on a common solution for tRNA substrate recognition.
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Registered trials
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 Socratic graph.