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Literature summary for 3.1.26.5 extracted from

  • Koutmou, K.S.; Zahler, N.H.; Kurz, J.C.; Campbell, F.E.; Harris, M.E.; Fierke, C.A.
    Protein-precursor tRNA contact leads to sequence-specific recognition of 5 leaders by bacterial ribonuclease P (2010), J. Mol. Biol., 396, 195-208.
    View publication on PubMedView publication on EuropePMC

Protein Variants

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

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

Organism UniProt Comment Textmining
Bacillus subtilis
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Escherichia coli
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Substrates and Products (Substrate)

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
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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
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Synonyms

Synonyms Comment Organism
ribonuclease P
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Bacillus subtilis
ribonuclease P
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Escherichia coli
RNase P
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Bacillus subtilis
RNase P
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Escherichia coli