Literature summary for 3.1.26.5 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.

Application

Application	Comment	Organism
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)

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

Crystallization (Commentary)

Crystallization (Comment)	Organism
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
full-length RNase P RNA of type B, to 3.3 A resolution	Geobacillus stearothermophilus

Crystallization (Comment)

Organism

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

full-length RNase P RNA of type B, to 3.3 A resolution

Geobacillus stearothermophilus

Inhibitors

Inhibitors	Comment	Organism	Structure
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

Metals/Ions	Comment	Organism	Structure
Mg2+	10 mM is optimal for the holoenzyme	Escherichia coli
Mg2+	60 mM is optimal for the holoenzyme	Bacillus subtilis

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	-	-	-
Escherichia coli	-	-	-
Geobacillus stearothermophilus	-	-	-
Mycoplasma genitalium	-	-	-
no activity in Nanoarchaeum equitans	-	-	-
Salmonella enterica subsp. enterica serovar Typhimurium	-	-	-
Thermotoga maritima	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
partially purified	Bacillus subtilis
partially purified by ion-exchange chromatography	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
pre-tRNA + H2O	catalyzes 5' maturation of tRNAs. RNA component of RNase P is essential for pre-tRNA cleavage	Escherichia coli	tRNA + 5'-oligoribonucleotide	-	?
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

Synonyms	Comment	Organism
M1 RNA	-	Escherichia coli
ribonuclease P	-	Salmonella enterica subsp. enterica serovar Typhimurium
ribonuclease P	-	Mycoplasma genitalium
ribonuclease P	-	Bacillus subtilis
ribonuclease P	-	Escherichia coli
ribonuclease P	-	Geobacillus stearothermophilus
ribonuclease P	-	Thermotoga maritima
RNase P	-	Salmonella enterica subsp. enterica serovar Typhimurium
RNase P	-	Mycoplasma genitalium
RNase P	-	Bacillus subtilis
RNase P	-	Escherichia coli
RNase P	-	Geobacillus stearothermophilus
RNase P	-	Thermotoga maritima
RNase P protein	-	Escherichia coli
RNase P RNA	-	Escherichia coli
RNase P RNA	-	Geobacillus stearothermophilus
RNase P RNA	-	Thermotoga maritima

Expression

Organism	Comment	Expression
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

General Information	Comment	Organism
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
physiological function	an in vitro transcribed RNase P RNA is catalytically active	Salmonella enterica subsp. enterica serovar Typhimurium
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
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