ArticleRNA (New York, N.Y.)2007
Probing the architecture of the B. subtilis RNase P holoenzyme active site by cross-linking and affinity cleavage.
Article in RNA (New York, N.Y.), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 36 citations in OpenAlex.
- Resurrecting the Activity of the RNA Subunit of Human RNase P.Chembiochem : a European journal of chemical biology · 2026Article
- 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
- Distributive enzyme binding controlled by local RNA context results in 3' to 5' directional processing of dicistronic tRNA precursors by Escherichia coli ribonuclease P.Nucleic acids research · 2019Article
- Analysis of the RNA Binding Specificity Landscape of C5 Protein Reveals Structure and Sequence Preferences that Direct RNase P Specificity.Cell chemical biology · 2016Article
- The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological Functions.Biomolecules · 2016Review
- M1 RNA is important for the in-cell solubility of its cognate C5 protein: Implications for RNA-mediated protein folding.RNA biology · 2015Article
- The bacterial ribonuclease P holoenzyme requires specific, conserved residues for efficient catalysis and substrate positioning.Nucleic acids research · 2012Article
- The RNR motif of B. subtilis RNase P protein interacts with both PRNA and pre-tRNA to stabilize an active conformer.RNA (New York, N.Y.) · 2011Article
- Probing the folding intermediate of Bacillus subtilis RNase P protein by nuclear magnetic resonance.Biochemistry · 2010Article
- Of proteins and RNA: the RNase P/MRP family.RNA (New York, N.Y.) · 2010Review
- A divalent cation stabilizes the active conformation of the B. subtilis RNase P x pre-tRNA complex: a role for an inner-sphere metal ion in RNase P.Journal of molecular biology · 2010Article
- The ancient history of the structure of ribonuclease P and the early origins of Archaea.BMC bioinformatics · 2010Article
- Protein-precursor tRNA contact leads to sequence-specific recognition of 5' leaders by bacterial ribonuclease P.Journal of molecular biology · 2010Article
- Binding of C5 protein to P RNA enhances the rate constant for catalysis for P RNA processing of pre-tRNAs lacking a consensus (+ 1)/C(+ 72) pair.Journal of molecular biology · 2010Article
- Solution structure of an archaeal RNase P binary protein complex: formation of the 30-kDa complex between Pyrococcus furiosus RPP21 and RPP29 is accompanied by coupled protein folding and highlights critical features for protein-protein and protein-RNA interactions.Journal of molecular biology · 2009Article
- Conformational change in the Bacillus subtilis RNase P holoenzyme--pre-tRNA complex enhances substrate affinity and limits cleavage rate.RNA (New York, N.Y.) · 2009Article
- Pre-tRNA turnover catalyzed by the yeast nuclear RNase P holoenzyme is limited by product release.RNA (New York, N.Y.) · 2009Article
- The putative RNase P motif in the DEAD box helicase Hera is dispensable for efficient interaction with RNA and helicase activity.Nucleic acids research · 2008Article
- Studies on Methanocaldococcus jannaschii RNase P reveal insights into the roles of RNA and protein cofactors in RNase P catalysis.Nucleic acids research · 2008Article
- Review
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Bacterial ribonuclease P (RNase P) is a ribonucleoprotein complex composed of one catalytic RNA (PRNA) and one protein subunit (P protein) that together catalyze the 5' maturation of precursor tRNA. High-resolution X-ray crystal structures of the individual P protein and PRNA components from several species have been determined, and structural models of the RNase P holoenzyme have been proposed. However, holoenzyme models have been limited by a lack of distance constraints between P protein and PRNA in the holoenzyme-substrate complex. Here, we report the results of extensive cross-linking and affinity cleavage experiments using single-cysteine P protein variants derivatized with either azidophenacyl bromide or 5-iodoacetamido-1,10-o-phenanthroline to determine distance constraints and to model the Bacillus subtilis holoenzyme-substrate complex. These data indicate that the evolutionarily conserved RNR motif of P protein is located near (<15 Angstroms) the pre-tRNA cleavage site, the base of the pre-tRNA acceptor stem and helix P4 of PRNA, the putative active site of the enzyme. In addition, the metal binding loop and N-terminal region of the P protein are proximal to the P3 stem-loop of PRNA. Studies using heterologous holoenzymes composed of covalently modified B. subtilis P protein and Escherichia coli M1 RNA indicate that P protein binds similarly to both RNAs. Together, these data indicate that P protein is positioned close to the RNase P active site and may play a role in organizing the RNase P active site.
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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.