ArticleJournal of molecular biology2010
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.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 24 citations in OpenAlex.
- 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
- Cryo-electron microscopy structure of an archaeal ribonuclease P holoenzyme.Nature communications · 2019Article
- 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
- The contribution of the C5 protein subunit ofRNA (New York, N.Y.) · 2017Article
- Analysis of the RNA Binding Specificity Landscape of C5 Protein Reveals Structure and Sequence Preferences that Direct RNase P Specificity.Cell chemical biology · 2016Article
- Differential substrate recognition by isozymes of plant protein-only Ribonuclease P.RNA (New York, N.Y.) · 2016Article
- Article
- Alternative substrate kinetics of Escherichia coli ribonuclease P: determination of relative rate constants by internal competition.The Journal of biological chemistry · 2013Article
- The bacterial ribonuclease P holoenzyme requires specific, conserved residues for efficient catalysis and substrate positioning.Nucleic acids research · 2012Article
- Fidelity of tRNA 5'-maturation: a possible basis for the functional dependence of archaeal and eukaryal RNase P on multiple protein cofactors.Nucleic acids research · 2012Article
- Cooperative RNP assembly: complementary rescue of structural defects by protein and RNA subunits of archaeal RNase P.Journal of molecular biology · 2011Article
- 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
- Archaeal/eukaryal RNase P: subunits, functions and RNA diversification.Nucleic acids research · 2010Review
- Dissecting functional cooperation among protein subunits in archaeal RNase P, a catalytic ribonucleoprotein complex.Nucleic acids research · 2010Article
- Of proteins and RNA: the RNase P/MRP family.RNA (New York, N.Y.) · 2010Review
- Protein-precursor tRNA contact leads to sequence-specific recognition of 5' leaders by bacterial ribonuclease P.Journal of molecular biology · 2010Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The RNA subunit of the ribonucleoprotein enzyme ribonuclease P (RNase P (P RNA) contains the active site, but binding of Escherichia coli RNase P protein (C5) to P RNA increases the rate constant for catalysis for certain pre-tRNA substrates up to 1000-fold. Structure-swapping experiments between a substrate that is cleaved slowly by P RNA alone (pre-tRNA(f-met605)) and one that is cleaved quickly (pre-tRNA(met608)) pinpoint the characteristic C(+1)/A(+72) base pair of initiator tRNA(f-met) as the sole determinant of slow RNA-alone catalysis. Unlike other substrate modifications that slow RNA-alone catalysis, the presence of a C(+1)/A(+72) base pair reduces the rate constant for processing at both correct and miscleavage sites, indicating an indirect but nonetheless important role in catalysis. Analysis of the Mg(2)(+) dependence of apparent catalytic rate constants for pre-tRNA(met608) and a pre-tRNA(met608) (+1)C/(+72)A mutant provides evidence that C5 promotes rate enhancement primarily by compensating for the decrease in the affinity of metal ions important for catalysis engendered by the presence of the CA pair. Together, these results support and extend current models for RNase P substrate recognition in which contacts involving the conserved (+1)G/C(+72) pair of tRNA stabilize functional metal ion binding. Additionally, these observations suggest that C5 protein has evolved to compensate for tRNA variation at positions important for binding to P RNA, allowing for tRNA specialization.
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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.