Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | the RNR motif enhances catalytic activity and substrate recognition, it enhances the affinity of RNase P for pre-tRNA involving residues R60 and R62, overview | Bacillus subtilis |
Protein Variants | Comment | Organism |
---|---|---|
K64C | site-directed mutagenesis of the RNR motif of P protein subunit, the mutant shows unaltered RNA binding kinetics compared to the wild-type enzyme | Bacillus subtilis |
K64C | site-directed mutagenesis of an RNR motif residue, the mutant shows altered binding affinity for the substrate and between its components compared to the wild-type enzyme | Bacillus subtilis |
additional information | RNR motif mutations do not alter the kinetics of pre-tRNA cleavage | Bacillus subtilis |
R60A | site-directed mutagenesis of the RNR motif of P protein subunit, the mutant shows unaltered RNA binding kinetics compared to the wild-type enzyme | Bacillus subtilis |
R60A | site-directed mutagenesis of an RNR motif residue, the mutant shows altered binding affinity for the substrate and between its components compared to the wild-type enzyme | Bacillus subtilis |
R62A | site-directed mutagenesis of the RNR motif of P protein subunit, the mutant shows unaltered RNA binding kinetics compared to the wild-type enzyme | Bacillus subtilis |
R62A | site-directed mutagenesis of an RNR motif residue, the mutant shows altered binding affinity for the substrate and between its components compared to the wild-type enzyme | Bacillus subtilis |
R65A | site-directed mutagenesis of the RNR motif of P protein subunit, the mutant shows unaltered RNA binding kinetics compared to the wild-type enzyme | Bacillus subtilis |
R65A | site-directed mutagenesis of an RNR motif residue, the mutant shows altered binding affinity for the substrate and between its components compared to the wild-type enzyme | Bacillus subtilis |
R65C | site-directed mutagenesis of the RNR motif of P protein subunit, the mutant shows unaltered RNA binding kinetics compared to the wild-type enzyme | Bacillus subtilis |
R65C | site-directed mutagenesis of an RNR motif residue, the mutant shows altered binding affinity for the substrate and between its components compared to the wild-type enzyme | Bacillus subtilis |
R68A | site-directed mutagenesis of the RNR motif of P protein subunit, the mutant shows unaltered RNA binding kinetics compared to the wild-type enzyme | Bacillus subtilis |
R68A | site-directed mutagenesis of an RNR motif residue, the mutant shows altered binding affinity for the substrate and between its components compared to the wild-type enzyme | Bacillus subtilis |
R68C | site-directed mutagenesis of the RNR motif of P protein subunit, the mutant shows unaltered RNA binding kinetics compared to the wild-type enzyme | Bacillus subtilis |
R68C | site-directed mutagenesis of an RNR motif residue, the mutant shows altered binding affinity for the substrate and between its components compared to the wild-type enzyme | Bacillus subtilis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | the RNR motif enhances the affinity of RNase P for pre-tRNA | Bacillus subtilis | |
additional information | - |
additional information | kinetics of wild-type and mutant enzymes, affinity of PRNA for P protein, and of RNase P for pre-tRNAAsp substrate, overview. Apparent pKa and pH-independent single-turnover rate constants for wild-type enzyme and mutants R60A and R62A in Mg(II) | Bacillus subtilis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | activates | Bacillus subtilis | |
Ca2+ | metal-stabilized conformational change in RNase P that accompanies substrate binding and is essential for efficient catalysis | Bacillus subtilis | |
Mg2+ | metal-stabilized conformational change in RNase P that accompanies substrate binding and is essential for efficient catalysis | Bacillus subtilis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Bacillus subtilis | ribonuclease P catalyzes the metal-dependent 5' end maturation of precursor tRNAs | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
ribonucleoprotein | the enzyme is composed of a catalytic RNA (PRNA) and a protein subunit (P protein) | Bacillus subtilis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | ribonuclease P catalyzes the metal-dependent 5' end maturation of precursor tRNAs | Bacillus subtilis | ? | - |
? | |
pre-tRNA + H2O | - |
Bacillus subtilis | tRNA + 5' leader of tRNA | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | in bacteria, RNase P is composed of a catalytic RNA, PRNA, and a protein subunit, P protein, necessary for function in vivo. The P protein enhances pre-tRNA affinity, selectivity, and cleavage efficiency, as well as modulates the cation requirement for RNase P function. Two residues, R60 and R62, in the most highly conserved region of the P protein, the RNR motif, R60-R68, stabilize PRNA complexes with both P protein and pre-tRNA. The RNR motif enhances a metal-stabilized conformational change in RNase P that accompanies substrate binding and is essential for efficient catalysis. Stabilization of this conformational change contributes to both the decreased metal requirement and the enhanced substrate recognition of the RNase P holoenzyme, illuminating the role of the most highly conserved region of P protein in the RNase P reaction pathway | Bacillus subtilis |
Synonyms | Comment | Organism |
---|---|---|
RNase P | - |
Bacillus subtilis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Bacillus subtilis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
assay at | Bacillus subtilis |
General Information | Comment | Organism |
---|---|---|
malfunction | mutations in the RNR motif of P protein alter the affinity of PRNA for P protein, and of RNase P for pre-tRNAAsp, overview | Bacillus subtilis |
additional information | in bacteria, RNase P is composed of a catalytic RNA, PRNA, and a protein subunit, P protein, necessary for function in vivo. The P protein enhances pre-tRNA affinity, selectivity, and cleavage efficiency, as well as modulates the cation requirement for RNase P function. The RNR motif enhances a metal-stabilized conformational change in RNase P that accompanies substrate binding and is essential for efficient catalysis | Bacillus subtilis |
additional information | in bacteria, RNase P is composed of a catalytic RNA and a protein subunit (P protein) necessary for function in vivo. The P protein enhances pre-tRNA affinity, selectivity, and cleavage efficiency, as well as modulates the cation requirement for RNase P function. The two residues R60 and R62 in the most highly conserved region of the P protein, the RNR motif formed by residues R60-R68, stabilize PRNA complexes with both P protein and pre-tRNA, overview. The RNR motif enhances a metal-stabilized conformational change in RNase P that accompanies substrate binding and is essential for efficient catalysis | Bacillus subtilis |
physiological function | the RNR motif of RNase P protein interacts with both catalytic RNA PRNA and pre-tRNA to stabilize an active conformer | Bacillus subtilis |
physiological function | ribonuclease P catalyzes the metal-dependent 5' end maturation of precursor tRNAs | Bacillus subtilis |