ArticleNucleic acids research2001
Modular construction for function of a ribonucleoprotein enzyme: the catalytic domain of Bacillus subtilis RNase P complexed with B. subtilis RNase P protein.
Article in Nucleic acids research, 2001. 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, 38 citations in OpenAlex.
- Catalytic RNA Oligomers Formed by Co-Oligomerization of a Pair of Bimolecular RNase P Ribozymes.Molecules (Basel, Switzerland) · 2022Article
- The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological Functions.Biomolecules · 2016Review
- Cleavage of model substrates by archaeal RNase P: role of protein cofactors in cleavage-site selection.Nucleic acids research · 2011Article
- Of proteins and RNA: the RNase P/MRP family.RNA (New York, N.Y.) · 2010Review
- Weighted bootstrapping: a correction method for assessing the robustness of phylogenetic trees.BMC evolutionary biology · 2010Article
- 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
- Protein-precursor tRNA contact leads to sequence-specific recognition of 5' leaders by bacterial ribonuclease P.Journal of molecular biology · 2010Article
- Evidence that substrate-specific effects of C5 protein lead to uniformity in binding and catalysis by RNase P.The EMBO journal · 2006Article
- Hybrid E. coli--Mitochondrial ribonuclease P RNAs are catalytically active.RNA (New York, N.Y.) · 2006Article
- Genes for small, noncoding RNAs under sporulation control in Bacillus subtilis.Journal of bacteriology · 2006Article
- Identification and analysis of ribonuclease P and MRP RNA in a broad range of eukaryotes.Nucleic acids research · 2005Article
- Ionic interactions between PRNA and P protein in Bacillus subtilis RNase P characterized using a magnetocapture-based assay.RNA (New York, N.Y.) · 2004Article
- Phylogenetic analysis of the structure of RNase MRP RNA in yeasts.RNA (New York, N.Y.) · 2002Article
- Eukaryotic ribonuclease P: a plurality of ribonucleoprotein enzymes.Annual review of biochemistry · 2002Review
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2 authors at 1 institution in 1 country.
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Abstract
The bacterial RNase P holoenzyme catalyzes the formation of the mature 5'-end of tRNAs and is composed of an RNA and a protein subunit. Among the two folding domains of the RNase P RNA, the catalytic domain (C-domain) contains the active site of this ribozyme. We investigated specific binding of the Bacillus subtilis C-domain with the B.subtilis RNase P protein and examined the catalytic activity of this C-domain-P protein complex. The C-domain forms a specific complex with the P protein with a binding constant of approximately 0.1 microM. The C-domain-P protein complex and the holoenzyme are equally efficient in cleaving single-stranded RNA (approximately 0.9 min(-1) at pH 7.8) and substrates with a hairpin-loop 3' to the cleavage site (approximately 40 min(-1)). The holoenzyme reaction is much more efficient with a pre-tRNA substrate, binding at least 100-fold better and cleaving 10-500 times more efficiently. These results demonstrate that the RNase P holoenzyme is functionally constructed in three parts. The catalytic domain alone contains the active site, but has little specificity and affinity for most substrates. The specificity and affinity for the substrate is generated by either the specificity domain of RNase P RNA binding to a T stem-loop-like hairpin or RNase P protein binding to a single-stranded RNA. This modular construction may be exploited to obtain RNase P-based ribonucleoprotein complexes with altered substrate specificity.
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