Cryo-electron microscopy structure of an archaeal ribonuclease P holoenzyme [PDF]
Nature Communications, 2019 Ribonulease P is a conserved ribozyme present in all kingdoms of life that is involved in the 5′ maturation step of tRNAs. Here the authors determine the structure of an archaeal RNase P holoenzyme that reveals how archaeal RNase P recognizes its tRNA ...
Futang Wan +8 more
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Comparison of participant-collected nasal and staff-collected oropharyngeal specimens for human ribonuclease P detection with RT-PCR during a community-based study. [PDF]
PLoS ONE, 2020 We analyzed 4,352 participant- and staff-collected respiratory specimens from 2,796 subjects in the Oregon Child Absenteeism due to Respiratory Disease Study.
Mitchell T Arnold +12 more
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Philosophical Transactions of the Royal Society B: Biological Sciences, 2011 The gene coding for the RNA subunit of ribonuclease P (RNase P) is essential in all free-living organisms. The RNA subunit, itself, is an enzyme and, from its evolutionary tree, we can infer that it is a very ancient molecule. The specificity of this enzyme is that it cleaves other RNA molecules at the junction of single-stranded and the 5′ end of ...
Altman S.
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Structural basis for protein-free catalysis by ribonuclease P ribozyme [PDF]
Nature CommunicationsRibonuclease P (RNase P) is an essential metallonuclease found in all three domains of life. However, the structural basis for the ancient RNase P RNA component acting alone as a ribozyme and catalytic metal-ion chemistry remains unknown.
Yun-Tzai Lee +9 more
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The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological Functions [PDF]
Biomolecules, 2016 Ribonuclease P (RNase P) is an essential endonuclease responsible for catalyzing 5’ end maturation in precursor transfer RNAs. Since its discovery in the 1970s, RNase P enzymes have been identified and studied throughout the three domains of life ...
Bradley P. Klemm +6 more
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Safety evaluation of the food enzyme ribonuclease P from the non‐genetically modified Penicillium citrinum strain AE‐RPE [PDF]
EFSA JournalThe food enzyme ribonuclease P (EC 3.1.26.5) is produced with the non‐genetically modified Penicillium citrinum strain AE‐RPE by Amano Enzyme Inc. It was considered free from viable cells of the production organism.
EFSA Panel on Food Enzymes (FEZ) +15 more
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The specificity landscape of bacterial ribonuclease P [PDF]
Journal of Biological ChemistryDeveloping 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, Alexandra R. +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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The ancient history of the structure of ribonuclease P and the early origins of Archaea [PDF]
BMC Bioinformatics, 2010 Background Ribonuclease P is an ancient endonuclease that cleaves precursor tRNA and generally consists of a catalytic RNA subunit (RPR) and one or more proteins (RPPs).
Sun Feng-Jie, Caetano-Anollés Gustavo
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Structure and Function of Eukaryotic Ribonuclease P RNA [PDF]
Molecular Cell, 2006 Ribonuclease P (RNase P) is the ribonucleoprotein endonuclease that processes the 5' ends of precursor tRNAs. Bacterial and eukaryal RNase P RNAs had the same primordial ancestor; however, they were molded differently by evolution. RNase P RNAs of eukaryotes, in contrast to bacterial RNAs, are not catalytically active in vitro without proteins.
Marquez, Steven M. +3 more
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