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Literature summary extracted from

  • McClain, W.H.; Lai, L.B.; Gopalan, V.
    Trials, travails and triumphs: an account of RNA catalysis in RNase P (2010), J. Mol. Biol., 397, 627-646.
    View publication on PubMed

Application

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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.26.5 Escherichia coli transformed with a plasmid expressing RNase P RNA Escherichia coli

Crystallization (Commentary)

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

Inhibitors

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

Metals/Ions

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

Organism

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
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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
-
 ?

Synonyms

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

Expression

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

General Information

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