Structure of a bacterial ribonuclease P holoenzyme in complex with tRNA. [PDF]
Nature, 2010 Ribonuclease (RNase) P is the universal ribozyme responsible for 5′-end tRNA processing. We report the crystal structure of the Thermotoga maritima RNase P holoenzyme in complex with tRNAPhe. The 154 kDa complex consists of a large catalytic RNA (P RNA),
Reiter NJ +5 more
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The specificity landscape of bacterial ribonuclease P. [PDF]
J Biol ChemDeveloping quantitative models of substrate specificity for RNA processing enzymes is a key step toward understanding their biology and guiding applications in biotechnology and biomedicine. Optimally, models to predict relative rate constants for alternative substrates should integrate an understanding of structures of the enzyme bound to "fast" and ...
Chamberlain AR +4 more
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Identification of the Acinetobacter baumannii Ribonuclease P Catalytic Subunit: Cleavage of a Target mRNA in the Presence of an External Guide Sequence [PDF]
Frontiers in Microbiology, 2018 The bacterial ribonuclease P or RNase P holoenzyme is usually composed of a catalytic RNA subunit, M1, and a cofactor protein, C5. This enzyme was first identified for its role in maturation of tRNAs by endonucleolytic cleavage of the pre-tRNA. The RNase
Carol Davies-Sala +6 more
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Eukaryotic Ribonuclease P: A Plurality of Ribonucleoprotein Enzymes [PDF]
Annual Review of Biochemistry, 2002 ▪ Abstract Ribonuclease P (RNase P) is an essential endonuclease that acts early in the tRNA biogenesis pathway. This enzyme catalyzes cleavage of the leader sequence of precursor tRNAs (pre-tRNAs), generating the mature 5′ end of tRNAs. RNase P activities have been identified in Bacteria, Archaea, and Eucarya, as well as organelles.
Shaohua Xiao +3 more
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The Ribonuclease P Database [PDF]
Nucleic Acids Research, 1996 Ribonuclease P is responsible for the 5'-maturation of tRNA precursors. Ribonuclease P is a ribonucleoprotein, and in bacteria (and some Archaea) the RNA subunit alone is catalytically active in vitro, i.e. it is a ribozyme. The Ribonuclease P Database is a compilation of ribonuclease P sequences, sequence alignments, secondary structures, three ...
James W. Brown
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Subsites for substrate recognition by bacterial ribonuclease P [PDF]
Nucleic Acids Symposium Series, 2008 We have prepared series of shape variant RNAs of a tRNA precursor and analyzed the substrate shape recognition by bacterial ribonuclease P ribozyme and holoenzyme. The results showed the evidence for the presence of subsites for the recognition of the trna shape.
Atsuko Fujimoto +4 more
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Bacterial RNA-free RNase P: Structural and functional characterization of multiple oligomeric forms of a minimal protein-only ribonuclease P. [PDF]
J Biol Chem, 2023 Wilhelm CA +10 more
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Inhibition of Murine Cytomegalovirus Infection in Animals by RNase P-Associated External Guide Sequences [PDF]
Molecular Therapy: Nucleic Acids, 2017 External guide sequence (EGS) RNAs are associated with ribonuclease P (RNase P), a tRNA processing enzyme, and represent promising agents for gene-targeting applications as they can direct RNase-P-mediated cleavage of a target mRNA.
Wei Li +9 more
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Modulation of ribonuclease P activity by calcipotriol [PDF]
European Journal of Biochemistry, 2000 The effects of cholesterol, 7‐dehydrocholesterol, vitamin D3 and several synthetic vitamin D3 analogs on ribonuclease P (RNase P) were investigated using a cell‐free system from the slime mold Dictyostelium discoideum. RNase P is an ubiquitous and essential enzyme that endonucleolytically cleaves all tRNA precursors to produce the mature 5′ end.
Evangelia Papadimou +4 more
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Ribonuclease P: function and variation.
Journal of Biological Chemistry, 1990 Norman R. Pace, Danielle Smith
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