Literature summary for 3.1.26.5 extracted from

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

Search for more literature for 3.1.26.5

Application

Application	Comment	Organism
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
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
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]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
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
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
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

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Posttranslational Modification

Posttranslational Modification	Comment	Organism
ribonucleoprotein	-	Thermus thermophilus
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
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
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)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	5'-endonucleolytic precursor tRNA cleavage	Bacillus subtilis	?	-	?
additional information	5'-endonucleolytic precursor tRNA cleavage	Thermus thermophilus	?	-	?
additional information	5'-endonucleolytic precursor tRNA cleavage	Escherichia coli	?	-	?
additional information	5'-endonucleolytic precursor tRNA cleavage	Aquifex aeolicus	?	-	?
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	?	-	?
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	?	-	?
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	?	-	?
additional information	substrate is a RNA-tRNA primary transcript	Thermus thermophilus	?	-	?
additional information	substrate is a RNA-tRNA primary transcript	Escherichia coli	?	-	?
precursor tRNA Gly + H2O	-	Aquifex aeolicus	mature tRNA Gly + 5'-GGAUUUUCCCUUUC	5' flank with homogeneous 3' end, CCAGUC-3'	?

Subunits

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

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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

General Information

General Information	Comment	Organism
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
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
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
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
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
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
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
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
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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)