ArticleNucleic acids research2005
RNase P: role of distinct protein cofactors in tRNA substrate recognition and RNA-based catalysis.
Article in Nucleic acids research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 25 citations in OpenAlex.
- Potential Applications of RNase P Ribozyme Against Hepatitis B Virus.Molecules (Basel, Switzerland) · 2025Review
- Review
- Human RNase P: overview of a ribonuclease of interrelated molecular networks and gene-targeting systems.RNA (New York, N.Y.) · 2023Review
- Mapping of RNase P Ribozyme Regions in Proximity with a Human RNase P Subunit Protein Using Fe(II)-EDTA Cleavage and Nuclease Footprint Analyses.Methods in molecular biology (Clifton, N.J.) · 2023Article
- The Dynamic Network of RNP RNase P Subunits.International journal of molecular sciences · 2021Review
- Riboswitches and the RNA world.Cold Spring Harbor perspectives in biology · 2012Review
- RNA binding properties of conserved protein subunits of human RNase P.Nucleic acids research · 2011Article
- The ancient history of the structure of ribonuclease P and the early origins of Archaea.BMC bioinformatics · 2010Article
- Interactions between subunits of Saccharomyces cerevisiae RNase MRP support a conserved eukaryotic RNase P/MRP architecture.Nucleic acids research · 2007Article
- Human RNase P: a tRNA-processing enzyme and transcription factor.Nucleic acids research · 2007Review
- Analysis of RNase P protein (rnpA) expression in Bacillus subtilis utilizing strains with suppressible rnpA expression.Journal of bacteriology · 2006Article
- Differential association of protein subunits with the human RNase MRP and RNase P complexes.RNA (New York, N.Y.) · 2006Article
- Ribonuclease P: the evolution of an ancient RNA enzyme.Critical reviews in biochemistry and molecular biologyArticle
- Development of RNase P ribozyme-based therapy against oral herpesvirus infections by HSV-1 and KSHV.International journal of immunopathology and pharmacologyReview
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Escherichia coli ribonuclease P (RNase P) has a protein component, termed C5, which acts as a cofactor for the catalytic M1 RNA subunit that processes the 5' leader sequence of precursor tRNA. Rpp29, a conserved protein subunit of human RNase P, can substitute for C5 protein in reconstitution assays of M1 RNA activity. To better understand the role of the former protein, we compare the mode of action of Rpp29 to that of the C5 protein in activation of M1 RNA. Enzyme kinetic analyses reveal that complexes of M1 RNA-Rpp29 and M1 RNA-C5 exhibit comparable binding affinities to precursor tRNA but different catalytic efficiencies. High concentrations of substrate impede the activity of the former complex. Rpp29 itself exhibits high affinity in substrate binding, which seems to reduce the catalytic efficiency of the reconstituted ribonucleoprotein. Rpp29 has a conserved C-terminal domain with an Sm-like fold that mediates interaction with M1 RNA and precursor tRNA and can activate M1 RNA. The results suggest that distinct protein folds in two unrelated protein cofactors can facilitate transition from RNA- to ribonucleoprotein-based catalysis by RNase P.
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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 OpenQuestion graph.