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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Safety evaluation of the food enzyme ribonuclease P from the non‐genetically modified Penicillium citrinum strain AE‐RP‐4 [PDF]
EFSA Journal, 2023 The food enzyme ribonuclease P (EC 3.1.26.5) is produced with the non‐genetically modified Penicillium citrinum strain AE‐RP‐4 by Amano Enzyme Inc. It is intended to be used in yeast processing only for the production of yeast extract.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP) +26 more
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Structural and mechanistic basis for recognition of alternative tRNA precursor substrates by bacterial ribonuclease P [PDF]
Nature Communications, 2022 Ribonuclease P efficiently processes all tRNA precursors despite sequence variation at the site of cleavage. Here, authors use high-throughput enzymology and cryoEM to reveal conformational changes that drive recognition by bacterial RNase P.
Jiaqiang Zhu +5 more
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New insights into the role of ribonuclease P protein subunit p30 from tumor to internal reference [PDF]
Frontiers in Oncology, 2022 Ribonuclease P protein subunit p30 (RPP30) is a highly conserved housekeeping gene that exists in many species and tissues throughout the three life kingdoms (archaea, bacteria, and eukaryotes).
Junchao Wu +7 more
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Journal of Biological Chemistry, 1996 Ribonuclease P (RNase P) is responsible for the generation of mature 5' termini of tRNA. The RNA component of this complex encodes the enzymatic activity in bacteria and is itself catalytically active under appropriate conditions in vitro. The role of the subunits in eucaryotes has not yet been established.
Heather L. True, Daniel W. Celander
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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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Philos Trans R Soc Lond B Biol Sci, 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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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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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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