ArticleRNA (New York, N.Y.)2004
Crystal structure of archaeal ribonuclease P protein Ph1771p from Pyrococcus horikoshii OT3: an archaeal homolog of eukaryotic ribonuclease P protein Rpp29.
Article in RNA (New York, N.Y.), 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 43 citations in OpenAlex.
- Cryo-electron microscopy structure of an archaeal ribonuclease P holoenzyme.Nature communications · 2019Article
- Sequence Analysis and Comparative Study of the Protein Subunits of Archaeal RNase P.Biomolecules · 2016Review
- Modular architecture of eukaryotic RNase P and RNase MRP revealed by electron microscopy.Nucleic acids research · 2012Article
- 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
- Assembly of the complex between archaeal RNase P proteins RPP30 and Pop5.Archaea (Vancouver, B.C.) · 2011Article
- 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
- 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
- Interactions between subunits of Saccharomyces cerevisiae RNase MRP support a conserved eukaryotic RNase P/MRP architecture.Nucleic acids research · 2007Article
- Functional reconstitution and characterization of Pyrococcus furiosus RNase P.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Functional characterization of the conserved amino acids in Pop1p, the largest common protein subunit of yeast RNases P and MRP.RNA (New York, N.Y.) · 2006Article
- Structure of Pfu Pop5, an archaeal RNase P protein.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- RNase P: role of distinct protein cofactors in tRNA substrate recognition and RNA-based catalysis.Nucleic acids research · 2005Article
- Ribonuclease P: the evolution of an ancient RNA enzyme.Critical reviews in biochemistry and molecular biologyArticle
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Authors and funding
5 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Ribonuclease P (RNase P) is the endonuclease responsible for the removal of 5' leader sequences from tRNA precursors. The crystal structure of an archaeal RNase P protein, Ph1771p (residues 36-127) from hyperthermophilic archaeon Pyrococcus horikoshii OT3 was determined at 2.0 A resolution by X-ray crystallography. The structure is composed of four helices (alpha1-alpha4) and a six-stranded antiparallel beta-sheet (beta1-beta6) with a protruding beta-strand (beta7) at the C-terminal region. The strand beta7 forms an antiparallel beta-sheet by interacting with strand beta4 in a symmetry-related molecule, suggesting that strands beta4 and beta7 could be involved in protein-protein interactions with other RNase P proteins. Structural comparison showed that the beta-barrel structure of Ph1771p has a topological resemblance to those of Staphylococcus aureus translational regulator Hfq and Haloarcula marismortui ribosomal protein L21E, suggesting that these RNA binding proteins have a common ancestor and then diverged to specifically bind to their cognate RNAs. The structure analysis as well as structural comparison suggested two possible RNA binding sites in Ph1771p, one being a concave surface formed by terminal alpha-helices (alpha1-alpha4) and beta-strand beta6, where positively charged residues are clustered. A second possible RNA binding site is at a loop region connecting strands beta2 and beta3, where conserved hydrophilic residues are exposed to the solvent and interact specifically with sulfate ion. These two potential sites for RNA binding are located in close proximity. The crystal structure of Ph1771p provides insight into the structure and function relationships of archaeal and eukaryotic RNase P.
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