ArticleNucleic acids research2012
The bacterial ribonuclease P holoenzyme requires specific, conserved residues for efficient catalysis and substrate positioning.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- RNase P cleavage of pseudoknot substrates reveals differences in active site architecture that depend on residue N-1 in the 5' leader.RNA biology · 2025Article
- TERRA-LSD1 phase separation promotes R-loop formation for telomere maintenance in ALT cancer cells.Nature communications · 2024Article
- Structural and mechanistic basis for recognition of alternative tRNA precursor substrates by bacterial ribonuclease P.Nature communications · 2022Article
- Dissecting Monomer-Dimer Equilibrium of an RNase P Protein Provides Insight Into the Synergistic Flexibility of 5' Leader Pre-tRNA Recognition.Frontiers in molecular biosciences · 2021Article
- A screening platform to monitor RNA processing and protein-RNA interactions in ribonuclease P uncovers a small molecule inhibitor.Nucleic acids research · 2019Article
- Crystal structure of the ribonuclease-P-protein subunit from Staphylococcus aureus.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Inner-Sphere Coordination of Divalent Metal Ion with Nucleobase in Catalytic RNA.Journal of the American Chemical Society · 2017Article
- The contribution of the C5 protein subunit ofRNA (New York, N.Y.) · 2017Article
- Structural Roles of Noncoding RNAs in the Heart of Enzymatic Complexes.Biochemistry · 2017Article
- Alternative substrate kinetics of Escherichia coli ribonuclease P: determination of relative rate constants by internal competition.The Journal of biological chemistry · 2013Article
- PPR proteins shed a new light on RNase P biology.RNA biology · 2013Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
RNase P is an RNA-based enzyme primarily responsible for 5'-end pre-tRNA processing. A structure of the bacterial RNase P holoenzyme in complex with tRNAPhe revealed the structural basis for substrate recognition, identified the active site location, and showed how the protein component increases functionality. The active site includes at least two metal ions, a universal uridine (U52), and P RNA backbone moieties, but it is unclear whether an adjacent, bacterially conserved protein loop (residues 52-57) participates in catalysis. Here, mutagenesis combined with single-turnover reaction kinetics demonstrate that point mutations in this loop have either no or modest effects on catalytic efficiency. Similarly, amino acid changes in the 'RNR' region, which represent the most conserved region of bacterial RNase P proteins, exhibit negligible changes in catalytic efficiency. However, U52 and two bacterially conserved protein residues (F17 and R89) are essential for efficient Thermotoga maritima RNase P activity. The U52 nucleotide binds a metal ion at the active site, whereas F17 and R89 are positioned >20 Å from the cleavage site, probably making contacts with N(-4) and N(-5) nucleotides of the pre-tRNA 5'-leader. This suggests a synergistic coupling between transition state formation and substrate positioning via interactions with the leader.
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Registered trials
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