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Literature summary for 3.1.26.5 extracted from

  • Koutmou, K.S.; Day-Storms, J.J.; Fierke, C.A.
    The RNR motif of B. subtilis RNase P protein interacts with both PRNA and pre-tRNA to stabilize an active conformer (2011), RNA, 17, 1225-1235.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.26.5

Activating Compound

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

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 [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

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
ribonucleoprotein the enzyme is composed of a catalytic RNA (PRNA) and a protein subunit (P protein) Bacillus subtilis

Substrates and Products (Substrate)

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

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

Synonyms Comment Organism
RNase P
-
 Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 assay at Bacillus subtilis

General Information

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