Protein Variants | Comment | Organism |
---|---|---|
F16A | affinity of RNase P for A(-4) pre-tRNA is decreased more than 10fold | Bacillus subtilis |
F16C | increases the affinity for G(-4) pre-tRNA by at least 25fold | Bacillus subtilis |
F20A | decrease in the affinity of A(-4) pre-tRNA compared to that of G(-4) pre-tRNA, causing the A(-4)/G(-4) selectivity ratio to decrease to less than 1. Mutations in the central cleft of P protein alters the observed cleavage rate constant by less than 2fold | Bacillus subtilis |
K64A | affinity of RNase P for A(-4) pre-tRNA is decreased | Bacillus subtilis |
N61A | affinity of RNase P for A(-4) pre-tRNA is decreased | Bacillus subtilis |
R60A | decrease in the affinity of A(-4) pre-tRNA compared to that of G(-4) pre-tRNA, causing the A(-4)/G(-4) selectivity ratio to decrease to less than 1 | Bacillus subtilis |
R65A | affinity of RNase P for A(-4) pre-tRNA is decreased more than 10fold | Bacillus subtilis |
Y34A | decrease in the affinity of A(-4) pre-tRNA compared to that of G(-4) pre-tRNA, causing the A(-4)/G(-4) selectivity ratio to decrease to less than 1. Mutations in the central cleft of P protein alters the observed cleavage rate constant by less than 2fold | Bacillus subtilis |
Y34F | decreases A(-4) pre-tRNA binding affinity, although to a smaller extent than mutant Y34A. Binds A(-4) and P(-4) pre-tRNAs with comparable affinities. Mutations in the central cleft of P protein alters the observed cleavage rate constant by less than 2fold | Bacillus subtilis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | stabilizes RNase P folding and substrate binding with little activation of catalytic activity. Affinity of RNase P for A(-4) pre-tRNA increases 4fold as the Ca2+ concentration increases from 2 mM to 5 mM. Affinity for the G(-4) substrate increases 65fold over the same range | Bacillus subtilis |
Organism | UniProt | Comment | Textmining |
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Bacillus subtilis | - |
- |
- |
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pre-tRNAAsp + H2O | pre-tRNA binding affinities for RNase P are enhanced by sequence-specific contacts between the fourth pre-tRNA nucleotide on the 5' side of the cleavage site (N(-4)) and the RNase P protein (P protein) subunit. RNase P has a higher affinity for pre-tRNA with adenosine at N(-4), and this binding preference is amplified at physiological divalent ion concentrations. Binds A(-4) pre-tRNA 20fold more tightly than the G(-4) substrate, and binds the C(-4) and U(-4) substrates with intermediate affinity. F20 and Y34 contribute to selectivity at N(-4). The hydroxyl group of Y34 enhances selectivity, likely by forming a hydrogen bond with the N(-4) nucleotide | Bacillus subtilis | tRNAAsp + 5'-oligoribonucleotide | - |
? | |
pre-tRNAAsp + H2O | pre-tRNA binding affinities for RNase P are enhanced by sequence-specific contacts between the fourth pre-tRNA nucleotide on the 5' side of the cleavage site (N(-4)) and the RNase P protein (P protein) subunit. Sequence preference of RNase P shows a weak preference for adenosine and cytosine at N(-4). Higher binding affinity for A(-4) and C(-4) pre-tRNAs relative to that for G(-4) and U(-4), with an overall preference of 5fold. L34 contributes to selectivity | Escherichia coli | tRNAAsp + 5'-oligoribonucleotide | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ribonuclease P | - |
Bacillus subtilis |
ribonuclease P | - |
Escherichia coli |
RNase P | - |
Bacillus subtilis |
RNase P | - |
Escherichia coli |