EC Number | Application | Comment | Organism |
---|---|---|---|
3.1.26.5 | medicine | ability to purify large amounts of M1 RNA, 20fold greater level from transformed cells than that from untransformed cells. M1GSs (tethered to the 3' end of M1 RNA by a spacer of 20-50 nt is a guide sequence (13-16 nt) that base pairs with the target RNA and has an unpaired 3'-RCCA needed for interacting with M1 RNA) degrades the oncogenic chimera BCR-ABL mRNA specifically and halted cancer development in mammalian cells when the guide sequence is designed to target the fusion region | Escherichia coli |
EC Number | Cloned (Comment) | Organism |
---|---|---|
3.1.26.5 | Escherichia coli transformed with a plasmid expressing RNase P RNA | Escherichia coli |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.1.26.5 | full-length RNase P RNA of type A, to 3.85 A resolution. Various coaxially stacked helices, held together by tertiary contacts, form the 3-D core that can be viewed as two single helix-thick tiers. Layer 1 encompasses both the substrate-binding regions and the putative catalytic center. Layer 2 serves as the platform for the larger layer 1 and contributes to the overall stability through tertiary interactions between the P8/P9 helical stack and the tetraloops L14 and L18. P8/P9 acts as a brace that brings together distal helices in the S (P13/P14 stack) and C domains (P18). The precise orientation of the S and C domains, facilitated by layer 2, underlies the exquisite inter-domain cooperation in substrate binding and catalysis | Thermotoga maritima |
3.1.26.5 | full-length RNase P RNA of type B, to 3.3 A resolution | Geobacillus stearothermophilus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.1.26.5 | additional information | Ca2+-dependent microccocal nuclease treatment abolishes RNase P activity. Precipitation of RNAs from a partially purified preparation of RNase P results in loss of activity | Escherichia coli |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.1.26.5 | Mg2+ | 10 mM is optimal for the holoenzyme | Escherichia coli | |
3.1.26.5 | Mg2+ | 60 mM is optimal for the holoenzyme | Bacillus subtilis |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.26.5 | Bacillus subtilis | - |
- |
- |
3.1.26.5 | Escherichia coli | - |
- |
- |
3.1.26.5 | Geobacillus stearothermophilus | - |
- |
- |
3.1.26.5 | Mycoplasma genitalium | - |
- |
- |
3.1.26.5 | no activity in Nanoarchaeum equitans | - |
- |
- |
3.1.26.5 | Salmonella enterica subsp. enterica serovar Typhimurium | - |
- |
- |
3.1.26.5 | Thermotoga maritima | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.1.26.5 | partially purified | Bacillus subtilis |
3.1.26.5 | partially purified by ion-exchange chromatography | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.26.5 | pre-tRNA + H2O | catalyzes 5' maturation of tRNAs. RNA component of RNase P is essential for pre-tRNA cleavage | Escherichia coli | tRNA + 5'-oligoribonucleotide | - |
? | |
3.1.26.5 | pre-tRNA + H2O | RNase P requires RNA for pre-tRNA processing. 2'-OH groups in the T stem-loop of the pre-tRNA that mediate contacts with the S-domain of the RNase P RNA | Bacillus subtilis | tRNA + 5'-oligoribonucleotide | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.26.5 | M1 RNA | - |
Escherichia coli |
3.1.26.5 | ribonuclease P | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
3.1.26.5 | ribonuclease P | - |
Mycoplasma genitalium |
3.1.26.5 | ribonuclease P | - |
Bacillus subtilis |
3.1.26.5 | ribonuclease P | - |
Escherichia coli |
3.1.26.5 | ribonuclease P | - |
Geobacillus stearothermophilus |
3.1.26.5 | ribonuclease P | - |
Thermotoga maritima |
3.1.26.5 | RNase P | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
3.1.26.5 | RNase P | - |
Mycoplasma genitalium |
3.1.26.5 | RNase P | - |
Bacillus subtilis |
3.1.26.5 | RNase P | - |
Escherichia coli |
3.1.26.5 | RNase P | - |
Geobacillus stearothermophilus |
3.1.26.5 | RNase P | - |
Thermotoga maritima |
3.1.26.5 | RNase P protein | - |
Escherichia coli |
3.1.26.5 | RNase P RNA | - |
Escherichia coli |
3.1.26.5 | RNase P RNA | - |
Geobacillus stearothermophilus |
3.1.26.5 | RNase P RNA | - |
Thermotoga maritima |
EC Number | Organism | Comment | Expression |
---|---|---|---|
3.1.26.5 | Escherichia coli | RNase P RNA expression decreases during the stringent response induced by amino acid starvation/cis-acting sequences in the RNase P RNA promoter | down |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.1.26.5 | malfunction | genetic alterations in either the RNA or protein subunit impair enzyme activity in vitro. A structural mutation in the RNase P protein (temperature-sensitive mutant ts241) affects the RNase P RNA level in vivo | Escherichia coli |
3.1.26.5 | physiological function | an in vitro transcribed RNase P RNA is catalytically active | Salmonella enterica subsp. enterica serovar Typhimurium |
3.1.26.5 | physiological function | assembly of the mature RNase P RNA with its cognate protein subunit ensures longevity of the holoenzyme complex in vivo. Increased growth rate of the organism coincides with increased RNase P RNA copy number | Escherichia coli |
3.1.26.5 | physiological function | RNase P is required in all free-living cells, RNase P is encoded even in the most compact bacterial genome of Mycoplasma genitalium | Mycoplasma genitalium |