Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | the pre-tRNA leaderprotein interaction decreases the observed dissociation rate of pre-tRNA from the isomerized enzyme-substrate complex | Bacillus subtilis |
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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | - |
- |
- |
Purification (Comment) | Organism |
---|---|
P protein purified by ion exchange chromatography under denaturing conditions | Bacillus subtilis |
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 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ribonuclease P | - |
Bacillus subtilis |
RNase P | - |
Bacillus subtilis |