ArticleNucleic acids research2008
Studies on Methanocaldococcus jannaschii RNase P reveal insights into the roles of RNA and protein cofactors in RNase P catalysis.
Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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35 citing papers in PubMed, 52 citations in OpenAlex.
- Crystal structures of type T archaeal ribonuclease P Rpp30, Rpp30/Pop5, and L7Ae provide insights into a reduced RNase P.Nucleic acids research · 2026Article
- Resurrecting the Activity of the RNA Subunit of Human RNase P.Chembiochem : a European journal of chemical biology · 2026Article
- Archaeal RNA processing and regulation: expanding the functional landscape.Microbiology and molecular biology reviews : MMBR · 2025Review
- Use of a small molecule microarray screen to identify inhibitors of the catalytic RNA subunit of Methanobrevibacter smithii RNase P.Nucleic acids research · 2025Article
- RNAs undergo phase transitions with lower critical solution temperatures.Nature chemistry · 2023Article
- Elucidation of structure-function relationships in Methanocaldococcus jannaschii RNase P, a multi-subunit catalytic ribonucleoprotein.Nucleic acids research · 2022Article
- New insights into the role of ribonuclease P protein subunit p30 from tumor to internal reference.Frontiers in oncology · 2022Review
- The many faces of RNA-based RNase P, an RNA-world relic.Trends in biochemical sciences · 2021Review
- 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
- 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
- Chance and necessity in the evolution of RNase P.RNA (New York, N.Y.) · 2018Article
- A novel double kink-turn module in euryarchaeal RNase P RNAs.Nucleic acids research · 2017Article
- Sequence Analysis and Comparative Study of the Protein Subunits of Archaeal RNase P.Biomolecules · 2016Review
- Functional implication of archaeal homologues of human RNase P protein pair Pop5 and Rpp30.Journal of biochemistry · 2016Article
- The L7Ae protein binds to two kink-turns in the Pyrococcus furiosus RNase P RNA.Nucleic acids research · 2014Article
- Molecular crowders and cosolutes promote folding cooperativity of RNA under physiological ionic conditions.RNA (New York, N.Y.) · 2014Article
- Conserved regions of ribonucleoprotein ribonuclease MRP are involved in interactions with its substrate.Nucleic acids research · 2013Article
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2 authors at 1 institution in 1 country.
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Abstract
Ribonuclease P (RNase P), a ribonucleoprotein (RNP) complex required for tRNA maturation, comprises one essential RNA (RPR) and protein subunits (RPPs) numbering one in bacteria, and at least four in archaea and nine in eukarya. While the bacterial RPR is catalytically active in vitro, only select euryarchaeal and eukaryal RPRs are weakly active despite secondary structure similarity and conservation of nucleotide identity in their putative catalytic core. Such a decreased archaeal/eukaryal RPR function might imply that their cognate RPPs provide the functional groups that make up the active site. However, substrate-binding defects might mask the ability of some of these RPRs, such as that from the archaeon Methanocaldococcus jannaschii (Mja), to catalyze precursor tRNA (ptRNA) processing. To test this hypothesis, we constructed a ptRNA-Mja RPR conjugate and found that indeed it self-cleaves efficiently (k(obs), 0.15 min(-1) at pH 5.5 and 55 degrees C). Moreover, one pair of Mja RPPs (POP5-RPP30) enhanced k(obs) for the RPR-catalyzed self-processing by approximately 100-fold while the other pair (RPP21-RPP29) had no effect; both binary RPP complexes significantly reduced the monovalent and divalent ionic requirement. Our results suggest a common RNA-mediated catalytic mechanism in all RNase P and help uncover parallels in RNase P catalysis hidden by plurality in its subunit make-up.
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