Structural and mechanistic basis for recognition of alternative tRNA precursor substrates by bacterial ribonuclease P [PDF]
Nature Communications, 2022 Binding of precursor tRNAs (ptRNAs) by bacterial ribonuclease P (RNase P) involves an encounter complex (ES) that isomerizes to a catalytic conformation (ES*).
Jiaqiang Zhu +5 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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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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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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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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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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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 previously uncharacterized RnpM (YlxR) protein modulates the activity of ribonuclease P in Bacillus subtilis in vitro. [PDF]
Nucleic Acids Res, 2023 Wicke D +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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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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