ArticleRNA (New York, N.Y.)2007
Evidence that binding of C5 protein to P RNA enhances ribozyme catalysis by influencing active site metal ion affinity.
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 29 papers.
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Who cites it
29 citing papers in PubMed, 49 citations in OpenAlex.
- Suppression of theRNA (New York, N.Y.) · 2024Article
- The previously uncharacterized RnpM (YlxR) protein modulates the activity of ribonuclease P in Bacillus subtilis in vitro.Nucleic acids research · 2024Article
- Structural and mechanistic basis for recognition of alternative tRNA precursor substrates by bacterial ribonuclease P.Nature communications · 2022Article
- Protein cofactors and substrate influence Mg2+-dependent structural changes in the catalytic RNA of archaeal RNase P.Nucleic acids research · 2021Article
- Purification, reconstitution, and mass analysis of archaeal RNase P, a multisubunit ribonucleoprotein enzyme.Methods in enzymology · 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 Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological Functions.Biomolecules · 2016Review
- Transcriptional control of an essential ribozyme in Drosophila reveals an ancient evolutionary divide in animals.PLoS genetics · 2015Article
- The L7Ae protein binds to two kink-turns in the Pyrococcus furiosus RNase P RNA.Nucleic acids research · 2014Article
- Nucleic acid catalysis: metals, nucleobases, and other cofactors.Chemical reviews · 2014Review
- 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
- Cleavage of model substrates by archaeal RNase P: role of protein cofactors in cleavage-site selection.Nucleic acids research · 2011Article
- Assembly of the complex between archaeal RNase P proteins RPP30 and Pop5.Archaea (Vancouver, B.C.) · 2011Article
- Of proteins and RNA: the RNase P/MRP family.RNA (New York, N.Y.) · 2010Review
- Ribosomal protein L7Ae is a subunit of archaeal RNase P.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The RNA subunit (P RNA) of the bacterial RNase P ribonucleoprotein is a ribozyme that catalyzes the Mg-dependent hydrolysis of pre-tRNA, but it requires an essential protein cofactor (P protein) in vivo that enhances substrate binding affinities and catalytic rates in a substrate dependent manner. Previous studies of Bacillus subtilis RNase P, containing a Type B RNA subunit, showed that its cognate protein subunit increases the affinity of metal ions important for catalysis, but the functional role of these ions is unknown. Here, we demonstrate that the Mg2+ dependence of the catalytic step for Escherichia coli RNase P, which contains a more common Type A RNA subunit, is also modulated by its cognate protein subunit (C5), indicating that this property is fundamental to P protein. To monitor specifically the binding of active site metal ions, we analyzed quantitatively the rescue by Cd2+ of an inhibitory Rp phosphorothioate modification at the pre-tRNA cleavage site. The results show that binding of C5 protein increases the apparent affinity of the rescuing Cd2+, providing evidence that C5 protein enhances metal ion affinity in the active site, and thus is likely to contribute significantly to rate enhancement at physiological metal ion concentrations.
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