ArticleNucleic acids research1996
The catalytic core of RNase P.
Article in Nucleic acids research, 1996. 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.
- Resurrecting the Activity of the RNA Subunit of Human RNase P.Chembiochem : a European journal of chemical biology · 2026Article
- Catalytic RNA Oligomers Formed by Co-Oligomerization of a Pair of Bimolecular RNase P Ribozymes.Molecules (Basel, Switzerland) · 2022Article
- Piece by piece: Building a ribozyme.The Journal of biological chemistry · 2020Review
- Cryo-electron microscopy structure of an archaeal ribonuclease P holoenzyme.Nature communications · 2019Article
- Critical domain interactions for type A RNase P RNA catalysis with and without the specificity domain.PloS one · 2018Article
- The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological Functions.Biomolecules · 2016Review
- Article
- Cleavage mediated by the P15 domain of bacterial RNase P RNA.Nucleic acids research · 2012Article
- Cleavage of model substrates by archaeal RNase P: role of protein cofactors in cleavage-site selection.Nucleic acids research · 2011Article
- Generation and development of RNA ligase ribozymes with modular architecture through "design and selection".Molecules (Basel, Switzerland) · 2010Review
- The ancient history of the structure of ribonuclease P and the early origins of Archaea.BMC bioinformatics · 2010Article
- Studies on Methanocaldococcus jannaschii RNase P reveal insights into the roles of RNA and protein cofactors in RNase P catalysis.Nucleic acids research · 2008Article
- Functional reconstitution and characterization of Pyrococcus furiosus RNase P.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Comparative photocross-linking analysis of the tertiary structures of Escherichia coli and Bacillus subtilis RNase P RNAs.The EMBO journal · 1998Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
A deletion mutant of the catalytic RNA component of Escherichia coli RNase P missing residues 87-241 retains the ability to interact with the protein component to form a functional catalyst. The deletion of this phylogenetically conserved region significantly increases the Km, indicating that the deleted structures may be important for binding to the precursor tRNA substrate but not for the cleavage reaction. Under some reaction conditions, this RNase P deletion mutant can become a relatively non-specific nuclease, indicating that this RNA's catalytic center may be more exposed. The catalytic core of the RNase P is formed by less than one third of the 377 residues of the RNase P RNA.
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Registered trials
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