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Literature summary extracted from

  • Goessringer, M.; Helmecke, D.; Hartmann, R.K.
    Characterization of RNase P RNA activity (2012), Methods Mol. Biol., 848, 61-72.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.1.26.5 synthesis the bacterial RNase P ribozyme might be used to release RNAs of interest with homogeneous 3'-OH ends from primary transcripts via site-specific cleavage, overview. Also, T7 transcription of mature tRNAs with clustered G residues at the 5'-end may result in 5'-end heterogeneities, which can be avoided by first transcribing the 5'-precursor tRNA (ptRNA) followed by P RNA-catalyzed processing to release the mature tRNA carrying a homogeneous 5'-monophosphate end Bacillus subtilis
3.1.26.5 synthesis the bacterial RNase P ribozyme might be used to release RNAs of interest with homogeneous 3'-OH ends from primary transcripts via site-specific cleavage, overview. Also, T7 transcription of mature tRNAs with clustered G residues at the 5'-end may result in 5'-end heterogeneities, which can be avoided by first transcribing the 5'-precursor tRNA (ptRNA) followed by P RNA-catalyzed processing to release the mature tRNA carrying a homogeneous 5'-monophosphate end Escherichia coli
3.1.26.5 synthesis the bacterial RNase P ribozyme might be used to release RNAs of interest with homogeneous 3'-OH ends from primary transcripts via site-specific cleavage, overview. Also, T7 transcription of mature tRNAs with clustered G residues at the 5'-end may result in 5'-end heterogeneities, which can be avoided by first transcribing the 5'-precursor tRNA (ptRNA) followed by P RNA-catalyzed processing to release the mature tRNA carrying a homogeneous 5'-monophosphate end Aquifex aeolicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.26.5 additional information
-
 additional information dissociation of the tRNA product from the catalytic RNA usually limits the rate of the RNA-alone reaction under multiple-turnover conditions, single-turnover conditions allow to analyze steps preceding product release Bacillus subtilis
3.1.26.5 additional information
-
 additional information dissociation of the tRNA product from the catalytic RNA usually limits the rate of the RNA-alone reaction under multiple-turnover conditions, single-turnover conditions allow to analyze steps preceding product release Aquifex aeolicus
3.1.26.5 additional information
-
 additional information dissociation of the tRNA product from the catalytic RNA usually limits the rate of the RNA-alone reaction under multiple-turnover conditions, single-turnover conditions allow to analyze steps preceding product release, pseudo-first-order rate constants of cleavage are calculated by nonlinear regression analysis Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.26.5 Mg2+ required Bacillus subtilis
3.1.26.5 Mg2+ required Thermus thermophilus
3.1.26.5 Mg2+ required Escherichia coli
3.1.26.5 Mg2+ required Aquifex aeolicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.26.5 additional information Bacillus subtilis 5'-endonucleolytic precursor tRNA cleavage ?
-
 ?
3.1.26.5 additional information Thermus thermophilus 5'-endonucleolytic precursor tRNA cleavage ?
-
 ?
3.1.26.5 additional information Escherichia coli 5'-endonucleolytic precursor tRNA cleavage ?
-
 ?
3.1.26.5 additional information Aquifex aeolicus 5'-endonucleolytic precursor tRNA cleavage ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.26.5 Aquifex aeolicus
-
-
-
3.1.26.5 Bacillus subtilis
-
-
-
3.1.26.5 Escherichia coli
-
 gene rnpB encoding the RNA subunit, gene rnpA encoding the protein subunit
-
3.1.26.5 Thermus thermophilus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.26.5 ribonucleoprotein
-
 Thermus thermophilus
3.1.26.5 ribonucleoprotein in bacteria, the enzyme is a ribonucleoprotein composed of two essential subunits: a catalytic RNA subunit and a single small protein cofactor, P protein, secondary structure and tertiary interactions, overview. The RNA subunit of bacterial RNase P is an efficient catalyst in vitro in the absence of its single protein cofactor, while the protein cofactor is essential for RNase P function in vivo, affecting the structure, function, and kinetics of the holoenzyme under physiological salt conditions Aquifex aeolicus
3.1.26.5 ribonucleoprotein the enzyme is a ribonucleoprotein composed of two essential subunits: a catalytic RNA subunit (P RNA, 350-400 nt) and a single small protein cofactor, P protein, secondary structure and tertiary interactions, overview. The RNA subunit of bacterial RNase P is an efficient catalyst in vitro in the absence of its single protein cofactor, while the protein cofactor is essential for RNase P function in vivo, affecting the structure, function, and kinetics of the holoenzyme under physiological salt conditions Bacillus subtilis
3.1.26.5 ribonucleoprotein the enzyme is a ribonucleoprotein composed of two essential subunits: a catalytic RNA subunit (P RNA, 350-400 nt) and a single small protein cofactor, P protein, secondary structure and tertiary interactions, overview. The RNA subunit of bacterial RNase P is an efficient catalyst in vitro in the absence of its single protein cofactor, while the protein cofactor is essential for RNase P function in vivo, affecting the structure, function, and kinetics of the holoenzyme under physiological salt conditions Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.26.5 additional information 5'-endonucleolytic precursor tRNA cleavage Bacillus subtilis ?
-
 ?
3.1.26.5 additional information 5'-endonucleolytic precursor tRNA cleavage Thermus thermophilus ?
-
 ?
3.1.26.5 additional information 5'-endonucleolytic precursor tRNA cleavage Escherichia coli ?
-
 ?
3.1.26.5 additional information 5'-endonucleolytic precursor tRNA cleavage Aquifex aeolicus ?
-
 ?
3.1.26.5 additional information in vitro, bacterial P RNA can catalyze tRNA maturation in the absence of the protein cofactor at elevated concentrations of mono- and divalent cations, thus acting as a trans-acting multiple-turnover ribozyme. Dissociation of the tRNA product from the catalytic RNA usually limits the rate of the RNA-alone reaction nder multiple-turnover conditions Bacillus subtilis ?
-
 ?
3.1.26.5 additional information in vitro, bacterial P RNA can catalyze tRNA maturation in the absence of the protein cofactor at elevated concentrations of mono- and divalent cations, thus acting as a trans-acting multiple-turnover ribozyme. Dissociation of the tRNA product from the catalytic RNA usually limits the rate of the RNA-alone reaction nder multiple-turnover conditions Aquifex aeolicus ?
-
 ?
3.1.26.5 additional information in vitro, bacterial P RNA can catalyze tRNA maturation in the absence of the protein cofactor at elevated concentrations of mono- and divalent cations, thus acting as a trans-acting multiple-turnover ribozyme. Dissociation of the tRNA product from the catalytic RNA usually limits the rate of the RNA-alone reaction under multiple-turnover conditions Escherichia coli ?
-
 ?
3.1.26.5 additional information substrate is a RNA-tRNA primary transcript Thermus thermophilus ?
-
 ?
3.1.26.5 additional information substrate is a RNA-tRNA primary transcript Escherichia coli ?
-
 ?
3.1.26.5 precursor tRNA Gly + H2O
-
 Aquifex aeolicus mature tRNA Gly + 5'-GGAUUUUCCCUUUC 5' flank with homogeneous 3' end, CCAGUC-3' ?

Subunits

EC Number Subunits Comment Organism
3.1.26.5 More enzyme secondary structure and tertiary interactions, overview Bacillus subtilis
3.1.26.5 More enzyme secondary structure and tertiary interactions, overview Escherichia coli
3.1.26.5 More enzyme secondary structure and tertiary interactions, overview Aquifex aeolicus

Synonyms

EC Number Synonyms Comment Organism
3.1.26.5 RNase P
-
 Bacillus subtilis
3.1.26.5 RNase P
-
 Thermus thermophilus
3.1.26.5 RNase P
-
 Escherichia coli
3.1.26.5 RNase P
-
 Aquifex aeolicus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.26.5 37
-
 assay at Aquifex aeolicus
3.1.26.5 37 55 assay at Escherichia coli
3.1.26.5 55
-
 assay at Thermus thermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.26.5 6
-
 assay at Aquifex aeolicus
3.1.26.5 7.4
-
 assay at Thermus thermophilus
3.1.26.5 7.4 7.5 assay at Escherichia coli

General Information

EC Number General Information Comment Organism
3.1.26.5 evolution two architectural subtypes of bacterial P RNAs, the phylogenetically prevailing ancestral type A represented by Escherichia coli P RNA, and Bacillus type B essentially confined to the low G + C Gram-positive bacteria, the prototype being Bacillus subtilis P RNA Bacillus subtilis
3.1.26.5 evolution two architectural subtypes of bacterial P RNAs, the phylogenetically prevailing ancestral type A represented by Escherichia coli P RNA, and Bacillus type B essentially confined to the low G + C Gram-positive bacteria, the prototype being Bacillus subtilis P RNA Escherichia coli
3.1.26.5 additional information in bacteria, the enzyme is a ribonucleoprotein composed of two essential subunits: a catalytic RNA subunit (P RNA, 350-400 nt) and a single small protein cofactor, P protein, secondary structure and tertiary interactions, overview. The RNA subunit of bacterial RNase P is an efficient catalyst in vitro in the absence of its single protein cofactor, while the protein cofactor is essential for RNase P function in vivo, affecting the structure, function, and kinetics of the holoenzyme under physiological salt conditions. In vitro, the protein subunit is dispensable, but its absence has to be compensated for by increased mono- and particularly divalent cations in order to achieve effi cient RNA-alone catalysis Escherichia coli
3.1.26.5 additional information in bacteria, the enzyme is a ribonucleoprotein composed of two essential subunits: a catalytic RNA subunit and a single small protein cofactor, P protein, secondary structure and tertiary interactions, overview. The RNA subunit of bacterial RNase P is an efficient catalyst in vitro in the absence of its single protein cofactor, while the protein cofactor is essential for RNase P function in vivo, affecting the structure, function, and kinetics of the holoenzyme under physiological salt conditions. In vitro, the protein subunit is dispensable, but its absence has to be compensated for by increased mono- and particularly divalent cations in order to achieve efficient RNA-alone catalysis Bacillus subtilis
3.1.26.5 additional information in bacteria, the enzyme is a ribonucleoprotein composed of two essential subunits: a catalytic RNA subunit and a single small protein cofactor, P protein, secondary structure and tertiary interactions, overview. The RNA subunit of bacterial RNase P is an efficient catalyst in vitro in the absence of its single protein cofactor, while the protein cofactor is essential for RNase P function in vivo, affecting the structure, function, and kinetics of the holoenzyme under physiological salt conditions. In vitro, the protein subunit is dispensable, but its absence has to be compensated for by increased mono- and particularly divalent cations in order to achieve efficient RNA-alone catalysis Aquifex aeolicus
3.1.26.5 physiological function the principle task of the ubiquitous enzyme RNase P is the generation of mature tRNA 5'-ends by removing precursor sequences from tRNA primary transcripts Bacillus subtilis
3.1.26.5 physiological function the principle task of the ubiquitous enzyme RNase P is the generation of mature tRNA 5'-ends by removing precursor sequences from tRNA primary transcripts Thermus thermophilus
3.1.26.5 physiological function the principle task of the ubiquitous enzyme RNase P is the generation of mature tRNA 5'-ends by removing precursor sequences from tRNA primary transcripts Escherichia coli
3.1.26.5 physiological function the principle task of the ubiquitous enzyme RNase P is the generation of mature tRNA 5'-ends by removing precursor sequences from tRNA primary transcripts Aquifex aeolicus