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Literature summary for 3.1.26.5 extracted from

  • Hsieh, J.; Fierke, C.A.
    Conformational change in the Bacillus subtilis RNase P holoenzyme-pre-tRNA complex enhances substrate affinity and limits cleavage rate (2009), RNA, 15, 1565-1577.
    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 pre-tRNA leader–protein interaction decreases the observed dissociation rate of pre-tRNA from the isomerized enzyme-substrate complex Bacillus subtilis

Application

Application Comment Organism
analysis fluorescein labeling has only a modest effect on the binding affinity of pre-tRNA and this fluorescent titration method may be useful for rapidly measuring the affinity of RNase P for a wide variety of substrates Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ time courses for fluorescein-labeled pre-tRNA binding to RNase P are biphasic in the presence of both Ca2+ and Mg2+II, requiring a minimal two-step association mechanism. With Ca2+, pre-tRNA cleavage is slow Bacillus subtilis
Mg2+ time courses for fluorescein-labeled pre-tRNA binding to RNase P are biphasic in the presence of both Ca2+ and Mg2+II, requiring a minimal two-step association mechanism. Cleavage rate constants are significantly higher in the presence of the physiologically important metal cofactor magnesium Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
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Purification (Commentary)

Purification (Comment) Organism
P protein purified by ion exchange chromatography under denaturing conditions Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pre-tRNAAsp + H2O pre-tRNA binds to RNase P using a two-step mechanism. Conformational change in the RNase P-pre-tRNA complex is coupled to the interactions between the 5' leader and P protein and aligns essential functional groups at the cleavage active site to enhance efficient cleavage of pre-tRNA Bacillus subtilis ?
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Synonyms

Synonyms Comment Organism
ribonuclease P
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 Bacillus subtilis
RNase P
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 Bacillus subtilis