ArticleProceedings of the National Academy of Sciences of the United States of America2003
Structure of Mth11/Mth Rpp29, an essential protein subunit of archaeal and eukaryotic RNase P.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. 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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27 citing papers in PubMed, 51 citations in OpenAlex.
- Protein cofactors and substrate influence Mg2+-dependent structural changes in the catalytic RNA of archaeal RNase P.Nucleic acids research · 2021Article
- 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
- Thermodynamics of coupled folding in the interaction of archaeal RNase P proteins RPP21 and RPP29.Biochemistry · 2012Article
- 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
- Assembly of the complex between archaeal RNase P proteins RPP30 and Pop5.Archaea (Vancouver, B.C.) · 2011Article
- Archaeal/eukaryal RNase P: subunits, functions and RNA diversification.Nucleic acids research · 2010Review
- Dissecting functional cooperation among protein subunits in archaeal RNase P, a catalytic ribonucleoprotein complex.Nucleic acids research · 2010Article
- 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
- Eukaryotic ribonucleases P/MRP: the crystal structure of the P3 domain.The EMBO journal · 2010Article
- Unexpected diversity of RNase P, an ancient tRNA processing enzyme: challenges and prospects.FEBS letters · 2010Review
- 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.Journal of molecular biology · 2009Article
- Solution structure of Pyrococcus furiosus RPP21, a component of the archaeal RNase P holoenzyme, and interactions with its RPP29 protein partner.Biochemistry · 2008Article
- Studies on the mechanism of inhibition of bacterial ribonuclease P by aminoglycoside derivatives.Nucleic acids research · 2008Article
- Solution NMR of large molecules and assemblies.Biochemistry · 2007Review
- Interactions between subunits of Saccharomyces cerevisiae RNase MRP support a conserved eukaryotic RNase P/MRP architecture.Nucleic acids research · 2007Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
We have determined the solution structure of Mth11 (Mth Rpp29), an essential subunit of the RNase P enzyme from the archaebacterium Methanothermobacter thermoautotrophicus (Mth). RNase P is a ubiquitous ribonucleoprotein enzyme primarily responsible for cleaving the 5' leader sequence during maturation of tRNAs in all three domains of life. In eubacteria, this enzyme is made up of two subunits: a large RNA ( approximately 120 kDa) responsible for mediating catalysis, and a small protein cofactor ( approximately 15 kDa) that modulates substrate recognition and is required for efficient in vivo catalysis. In contrast, multiple proteins are associated with eukaryotic and archaeal RNase P, and these proteins exhibit no recognizable homology to the conserved bacterial protein subunit. In reconstitution experiments with recombinantly expressed and purified protein subunits, we found that Mth Rpp29, a homolog of the Rpp29 protein subunit from eukaryotic RNase P, is an essential protein component of the archaeal holoenzyme. Consistent with its role in mediating protein-RNA interactions, we report that Mth Rpp29 is a member of the oligonucleotide/oligosaccharide binding fold family. In addition to a structured beta-barrel core, it possesses unstructured N- and C-terminal extensions bearing several highly conserved amino acid residues. To identify possible RNA contacts in the protein-RNA complex, we examined the interaction of the 11-kDa protein with the full 100-kDa Mth RNA subunit by using NMR chemical shift perturbation. Our findings represent a critical step toward a structural model of the RNase P holoenzyme from archaebacteria and higher organisms.
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