ArticleJournal of molecular biology2009
Solution structure of an archaeal RNase P binary protein complex: formation of the 30-kDa complex between Pyrococcus furiosus RPP21 and RPP29 is accompanied by coupled protein folding and highlights critical features for protein-protein and protein-RNA interactions.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 39 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
- 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
- In vitro reconstitution and analysis of eukaryotic RNase P RNPs.Nucleic acids research · 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
- The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological Functions.Biomolecules · 2016Review
- Sequence Analysis and Comparative Study of the Protein Subunits of Archaeal RNase P.Biomolecules · 2016Review
- The L7Ae protein binds to two kink-turns in the Pyrococcus furiosus RNase P RNA.Nucleic acids research · 2014Article
- Uncovering the stoichiometry of Pyrococcus furiosus RNase P, a multi-subunit catalytic ribonucleoprotein complex, by surface-induced dissociation and ion mobility mass spectrometry.Angewandte Chemie (International ed. in English) · 2014Article
- 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
- Modular architecture of eukaryotic RNase P and RNase MRP revealed by electron microscopy.Nucleic acids research · 2012Article
- Structural organizations of yeast RNase P and RNase MRP holoenzymes as revealed by UV-crosslinking studies of RNA-protein interactions.RNA (New York, N.Y.) · 2012Article
- Thermodynamics of coupled folding in the interaction of archaeal RNase P proteins RPP21 and RPP29.Biochemistry · 2012Article
- Interactions of a Pop5/Rpp1 heterodimer with the catalytic domain of RNase MRP.RNA (New York, N.Y.) · 2011Article
- Cooperative RNP assembly: complementary rescue of structural defects by protein and RNA subunits of archaeal RNase P.Journal of molecular biology · 2011Article
- RNA binding properties of conserved protein subunits of human RNase P.Nucleic acids research · 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
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Ribonuclease P (RNase P) is a ribonucleoprotein (RNP) enzyme that catalyzes the Mg(2+)-dependent 5' maturation of precursor tRNAs. In all domains of life, it is a ribozyme: the RNase P RNA (RPR) component has been demonstrated to be responsible for catalysis. However, the number of RNase P protein subunits (RPPs) varies from 1 in bacteria to 9 or 10 in eukarya. The archaeal RPR is associated with at least 4 RPPs, which function in pairs (RPP21-RPP29 and RPP30-POP5). We used solution NMR spectroscopy to determine the three-dimensional structure of the protein-protein complex comprising Pyrococcus furiosus RPP21 and RPP29. We found that the protein-protein interaction is characterized by coupled folding of secondary structural elements that participate in interface formation. In addition to detailing the intermolecular contacts that stabilize this 30-kDa binary complex, the structure identifies surfaces rich in conserved basic residues likely vital for recognition of the RPR and/or precursor tRNA. Furthermore, enzymatic footprinting experiments allowed us to localize the RPP21-RPP29 complex to the specificity domain of the RPR. These findings provide valuable new insights into mechanisms of RNP assembly and serve as important steps towards a three-dimensional model of this ancient RNP enzyme.
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