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Information on EC 3.1.26.5 - ribonuclease P and Organism(s) Bacillus subtilis and UniProt Accession P25814
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3.1.26.5 ribonuclease PSpecify your search results
Word Map
- 3.1.26.5
- ribonucleoproteins
- pre-trnas
-
endoribonuclease
-
endonucleolytic
- eculizumab
- aminoacylation
-
rna-based
-
stem-loops
-
phosphodiester
-
nucleolar
-
nocturnal
-
eubacterial
-
paroxysmal
-
gene-targeting
-
anticodon
-
base-pairing
-
rna-protein
- sars-cov-2
- c5a
- horikoshii
- hemoglobinuria
-
trna-like
- pyrococcus
-
swab
-
3'-terminal
-
5\'-leader
- riboswitches
- trnatyr
-
2'-hydroxyls
- trnahis
- trailer
-
cloverleaf
-
rna-rna
-
self-splicing
-
protein-rna
- tmrna
-
micrococcal
-
self-cleaving
-
t-loops
-
p-mediated
-
complement-mediated
- ncrnas
-
pseudoknots
-
watson-crick
-
eukaryal
- oligoribonucleotides
- analysis
- pharmacology
-
snornps
- synthesis
- medicine
- biotechnology
-
trnase
The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
Synonyms
rnase p, rnase p rna, rnase mrp, ribonuclease p, m1 rna, c5 protein, rnase p protein, rnase p holoenzyme, rpp30, protein c5, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
hPOP1
-
-
-
-
hPOP4
-
-
-
-
hPOP7
-
-
-
-
nuclease, ribo-, P
-
-
-
-
Protein C5
-
-
-
-
ribonuclease P
RNA processing protein POP1
-
-
-
-
RNA processing protein POP5
-
-
-
-
RNA processing protein POP6
-
-
-
-
RNA processing protein POP7
-
-
-
-
RNA processing protein POP8
-
-
-
-
RNase P
RNase P protein
-
-
-
-
RNaseP protein
-
-
-
-
RNaseP protein p20
-
-
-
-
RNaseP protein p30
-
-
-
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RNaseP protein p38
-
-
-
-
RNaseP protein p40
-
-
-
-
ribonuclease P
-
-
-
-
RNase P
-
-
-
-
RNase P
-
-
RNase P
-
the holoenzyme consists of two RNase P RNA and two protein subunits
RNase P
-
the RNase P holoenzyme is composed of RNase P RNA and a variable number of P protein subunits
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules structure-function study, substrate recognition and catalytic mechanism of the ribozyme
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, cleavage of ssRNA, mechanism
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, substrate recognition mechanism, detection methods, the RNA and protein subunits cooperate to bind different portions of the substrate structure, with the RNA subunit predominantly interacting with the mature domain of tRNA and the protein interacting with the 5'-leader sequence, substrate recognition and binding, reaction mechanism and detection methods
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, substrate recognition, enzyme possesses a single-stranded RNA binding cleft that interacts with the unpaired 5'-leader
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, the protein subunit is essential for substrate binding, the RNA subunit is essential for catalysis
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, the RNA subunit is essential for catalytic activity, divalent metal ion-dependent in-line SN2 displacement mechanism
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, tRNA precursor substrate recognition and cleavage mechanism, CR-IV region is imporatnt for tRNA binding
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
CAS REGISTRY NUMBER
COMMENTARY
71427-00-4
not distinguished from EC 3.1.26.7
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4.5S RNA, precursor to + H2O
?
-
enzyme complex formed with M1 RNA from E. coli and the protein moiety from E. coli or Bacillus subtilis are active. No activity with the enzyme complex formed with M1 RNA from Bacillus subtilis and the protein from either bacterial species
-
-
?
human pre-tRNATyr + H2O
human mature tRNATyr + 5'-oligonucleotide
-
-
-
-
?
pbuE adenine riboswitch + H2O
?
-
RNase P cleaves in vitro the adenine riboswitch upstream of the pbuE gene which codes for an adenine efflux pump
-
-
?
pre-tRNA mimic + H2O
?
-
small bipartite model substrates with different numbering of stem and 5'-flank base pairs, specific trans-cleavage at the canonical enzyme cleavage site, overview
-
-
?
pre-tRNA mimic a + H2O
?
-
mimic of natural enzyme substrate consisting of a 7 bp stem and a 3 nucleotide 5'-flank
-
-
?
pre-tRNA mimic b + H2O
?
-
mimic of natural enzyme substrate consisting of a 7 bp stem and a 1 nucleotide 5'-flank
-
-
?
pre-tRNA mimic c + H2O
?
-
mimic of natural enzyme substrate consisting of a 4 bp stem and a 3 nucleotide 5'-flank
-
-
?
pre-tRNA mimic d + H2O
?
-
mimic of natural enzyme substrate consisting of a 4 bp stem and a 1 nucleotide 5'-flank
-
-
?
ssRNA oligonucleotide + H2O
5'-phospho-3'-hydroxy-ribonucleotides
-
holoenzyme, specificity with different ssRNA substrates, determination of cleavage sites, overview
-
-
?
tRNAAsp precursor + H2O
mature tRNAAsp + 5'-terminal oligonucleotide
-
sequence
5'-terminal oligonucleotide with 3'-hydroxyl and 5'-phosphoryl
-
ir
tRNATyr precursor + H2O
mature tRNATyr + 5'-oligonucleotide
-
human substrate, cleavage of 5'-terminal oligonucleotide, enzyme recognizes the RNA substrate hairpin structure
generates 5'-phosphate,3'-hydroxyl-product
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
the enzyme is responsible for the cleavage of sequences from the 5' ends of precursors of tRNAs to produce the mature 5' terminus of the tRNA molecules
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
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
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
RNA moiety can cleave pre-rRNA in buffers containing either 60 mM Mg2+ or 10 mM Mg2+ plus 1 mM spermidine
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
cleavage of pre-tRNAAsp catalyzed by circular RNase P RNA is slightly faster than with the linear form
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
the conserved sequences CCA and GUUCG, as well as the substrate bond, occur on the same face of the coaxial helix that constitutes the minimum substrate for the enzyme
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
Gln-Leu tRNA dimeric precursor from bacteriophage T4-infected E. coli
-
-
?
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
-
-
?
pre-tRNAAsp + H2O
?
-
5' fluorescein-labeled Bacillus subtilis pre-tRNAAsp (Fl-pre-tRNA) possessing a 5-nucleotide leader
-
-
?
pre-tRNAAsp + H2O
tRNAAsp + 5'-oligoribonucleotide
-
5' leader segment directly interacts with P protein. The P protein binds to the 5' leader between the fourth and seventh nucleotides upstream of the cleavage site, extending the leader and decreasing its structural dynamics
-
-
?
pre-tRNAAsp + H2O
tRNAAsp + 5'-oligoribonucleotide
-
pre-tRNA binding affinities for RNase P are enhanced by sequence-specific contacts between the fourth pre-tRNA nucleotide on the 5' side of the cleavage site (N(-4)) and the RNase P protein (P protein) subunit. RNase P has a higher affinity for pre-tRNA with adenosine at N(-4), and this binding preference is amplified at physiological divalent ion concentrations. Binds A(-4) pre-tRNA 20fold more tightly than the G(-4) substrate, and binds the C(-4) and U(-4) substrates with intermediate affinity. F20 and Y34 contribute to selectivity at N(-4). The hydroxyl group of Y34 enhances selectivity, likely by forming a hydrogen bond with the N(-4) nucleotide
-
-
?
precursor tRNA + H2O
?
-
catalyze the 5' maturation of precursor tRNA
-
-
?
precursor tRNA + H2O
?
-
cleavage of precursor tRNAs with an LNA (extra methylene), 2'-OCH3, 2'-H or 2'-F modification at the canonical (c0) site by type B RNase P RNA. Extent of cleavage for the LNA (T-1) and 2'-OCH3 (T-1) substrates is extremely low. Weak cleavage of the 2'-OCH3 substrate at the c0 site. Stronger defect caused by 2'-H at nt -1 as compared to the Escherichia coli holoenzyme
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide, maturation
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide, maturation, essential
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
essential enzymes in the biogenesis of tRNA, maturation
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
tRNA processing
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide, cleavage site
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
site-specific cleavage of 5'-terminal oligonucleotide from pre-tRNA, 3 potential RNA binding motifs
generates 5'-phosphate,3'-hydroxyl-product
-
?
additional information
?
-
-
other pre-RNAs are also physiological substrates of the enzyme
-
-
?
additional information
?
-
-
substrate specificity is determined by the enzymes' RNA fold, the structure of the specificity domain of the RNA subunit provides the basis of understanding the structurs of other bacterial ribozyme molecules because all bacterial S domains havea common core that comprises stems P7-P11 plus J11/12-J12/11 module, overview
-
-
?
additional information
?
-
-
enzymatic and chemical protection, cross-linking of enzyme and substrate for determination of binding features, overview, the RNA subunit is the catalytic subunit, while the protein subunits are essential for substrate binding, broad substrate specificity
-
-
?
additional information
?
-
-
structural basis and mechanism of substrate specificity, global structure of the enzyme-substrate complex
-
-
?
additional information
?
-
-
substitution of a sulfur atom for either the Rp or Sp nonbridging phosphate oxygen or the 3'oxyanion leaving group in pre-tRNA decreases the catalytic rate constant by over 1000fold
-
-
?
additional information
?
-
-
substrate requirements for trans-cleavage of wild-type and mutant hybrid enzymes, overview
-
-
?
additional information
?
-
-
the RNA subunit can cleave tRNA substrate in absence of the protein subunit
-
-
?
additional information
?
-
-
catalyzes the 5-end maturation of tRNAs in all Kingdoms of life
-
-
?
additional information
?
-
-
the guanine riboswitch encoded upstream of xpt-pbuX operon, is not cleaved
-
-
?
additional information
?
-
-
5'-endonucleolytic precursor tRNA cleavage
-
-
?
additional information
?
-
-
ribonuclease P catalyzes the metal-dependent 5' end maturation of precursor tRNAs
-
-
?
additional information
?
-
-
the enzyme catalyzes the 5' end maturation of precursor tRNAs (pre-tRNAs)
-
-
?
additional information
?
-
-
in vitro, bacterial P RNA can catalyze tRNA maturation in the absence of the protein cofactor at elevated concentrations of mono- and divalent cations, thus acting as a trans-acting multiple-turnover ribozyme. Dissociation of the tRNA product from the catalytic RNA usually limits the rate of the RNA-alone reaction nder multiple-turnover conditions
-
-
?
additional information
?
-
-
the enzyme catalyzes the 5' end maturation of precursor tRNAs (pre-tRNAs). Inner-sphere coordination of divalent metal ions to PRNA is essential for catalytic activity, but not for the formation of the RNase P-pre-tRNA complex, which undergoes an essential conformational change before the cleavage step
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
precursor tRNA + H2O
?
-
catalyze the 5' maturation of precursor tRNA
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
the enzyme is responsible for the cleavage of sequences from the 5' ends of precursors of tRNAs to produce the mature 5' terminus of the tRNA molecules
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide, maturation
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide, maturation, essential
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
essential enzymes in the biogenesis of tRNA, maturation
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
tRNA processing
-
-
?
additional information
?
-
-
other pre-RNAs are also physiological substrates of the enzyme
-
-
?
additional information
?
-
-
substrate specificity is determined by the enzymes' RNA fold, the structure of the specificity domain of the RNA subunit provides the basis of understanding the structurs of other bacterial ribozyme molecules because all bacterial S domains havea common core that comprises stems P7-P11 plus J11/12-J12/11 module, overview
-
-
?
additional information
?
-
-
catalyzes the 5-end maturation of tRNAs in all Kingdoms of life
-
-
?
additional information
?
-
-
5'-endonucleolytic precursor tRNA cleavage
-
-
?
additional information
?
-
-
ribonuclease P catalyzes the metal-dependent 5' end maturation of precursor tRNAs
-
-
?
additional information
?
-
-
the enzyme catalyzes the 5' end maturation of precursor tRNAs (pre-tRNAs)
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Mn2+
NH4+
Zn2+
-
Zn2+ is involved in inner-sphere interactions with the P4 helix mimic of RNase P, the bound Zn2+ exhibits six-coordinate geometry with an average Zn2+-O/N bond distance of 2.08 A
additional information
Ca2+
-
suppresses enzyme activity, but supports RNA folding and substrate binding, used for binding assays
Ca2+
-
presence of the protein cofactor increases and equalizes substrate affinity and abolishes the substrate affinity differences seen for Escherichia coli relative to Bacillus subtilis P RNA
Ca2+
-
stabilizes RNase P folding and substrate binding with little activation of catalytic activity. Affinity of RNase P for A(-4) pre-tRNA increases 4fold as the Ca2+ concentration increases from 2 mM to 5 mM. Affinity for the G(-4) substrate increases 65fold over the same range
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
Ca2+
-
a divalent cation stabilizes the active conformation of the RNase P-pre-tRNA complex, a role for an inner-sphere metal ion, Mg2+ or Ca2+, in the enzyme. Structural changes that occur upon binding Ca(II) to the ES complex are determined by time-resolved FRET measurements of the distances between donor/acceptor fluorophores introduced at specific locations on the P protein and pre-tRNA 5' leader. The value of KD,obs has an apparent hyperbolic dependence on the concentration of calcium with an apparent dissociation constant for Ca(II) of 0.04 mM
Ca2+
-
metal-stabilized conformational change in RNase P that accompanies substrate binding and is essential for efficient catalysis
Mg2+
-
strict requirement for a divalent cation, Mg2+ or Mn2+. Hexacoordinated Mg2+ binds to the catalytic site on M1 RNA
Mg2+
-
absolutely required, optimal at about 20 mM, for catalysis and substrate shape recognition, influences substrate binding affinity
Mg2+
-
best metal ion, required for folding of the RNA, for binding of protein and substrate, and for catalytic activity
Mg2+
-
potential catalytic transition state structure including 3 required divalent metal ions, coordinated to nonbinding phosphate group oxygens
Mg2+
-
enzymatic activity depends on the presence of divalent metal ions such as Mg2+
Mg2+
-
significant association of Mg2+ ions at the P4 major groove of RNase P near the flexible pivot point (A5, G22, and G23)
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
Mg2+
-
a divalent cation stabilizes the active conformation of the RNase P-pre-tRNA complex, a role for an inner-sphere metal ion, Mg2+ or Ca2+, in the enzyme. A second, lower affinity Mg(II) activates cleavage catalyzed by the enzyme
Mg2+
-
metal-stabilized conformational change in RNase P that accompanies substrate binding and is essential for efficient catalysis
Mn2+
-
substitution of Mg2+ by Mn2+ can result in miscleavage of the substrate containing a N(-1)/N(73) pair, better sulfur coordination compared to Mg2+
Mn2+
-
Mn2+ paramagnetic line broadening experiments reveal strong metal localization at residues corresponding to G378 and G379
additional information
-
divalent metal cations are essential for catalysis and stabilize the enzyme conformation and subunit interaction
additional information
-
divalent metal ions are absolutely required, reduced activity with Ca2+
additional information
-
divalent metal ions are important cofactors for the catalytic reaction and for substrate binding at the conserved loops CR-II and CR-III in proximity to the substrate aminoacyl stem, enhancement of substrate affinity by 1000fold
additional information
-
enzyme is dependent on divalent metal ions, enzyme contains a metal binding loop
additional information
-
catalysis of pre-tRNA cleavage by RNase P requires at least one divalent cation capable of forming inner-sphere coordination, such as Mg2+, Mn2+, Zn2+ or Ca2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ca2+
-
suppresses enzyme activity, but supports RNA folding and substrate binding, used for binding assays
additional information
-
substitution of a sulfur atom for either the Rp or Sp nonbridging phosphate oxygen or the 3'oxyanion leaving group in pre-tRNA decreases the catalytic rate constant by over 1000fold
-
additional information
-
aminoglycoside-arginine conjugates and aminoglycoside poly-arginine conjugates can inhibit RNase P activity by interacting with the P protein/pre-tRNA binding site of PRNA, competing with the P protein for binding PRNA, and/or by displacing Mg2+ ions near the PRNA P15 loop leading to interference with RNase P catalysis
-
additional information
-
oligonucleotides targeting P15, but not those directed against P5.1 efficiently anneal to P RNA and inhibit activity (IC50 of about 2 nM) when incubated with preassembled Bacillus subtilis RNase P holoenzymes
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the pre-tRNA leaderprotein interaction decreases the observed dissociation rate of pre-tRNA from the isomerized enzyme-substrate complex
-
additional information
-
the RNR motif enhances catalytic activity and substrate recognition, it enhances the affinity of RNase P for pre-tRNA involving residues R60 and R62, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics, the rate constant for the scissile bond cleavage is pH-dependent
-
additional information
additional information
-
the RNR motif enhances the affinity of RNase P for pre-tRNA
-
additional information
additional information
-
dissociation of the tRNA product from the catalytic RNA usually limits the rate of the RNA-alone reaction under multiple-turnover conditions, single-turnover conditions allow to analyze steps preceding product release
-
additional information
additional information
-
kinetics and kinetic mechanism of reaction and enzyme stablization with metal ions, overview
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes, affinity of PRNA for P protein, and of RNase P for pre-tRNAAsp substrate, overview. Apparent pKa and pH-independent single-turnover rate constants for wild-type enzyme and mutants R60A and R62A in Mg(II)
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
-
mutations in the RNR motif of P protein alter the affinity of PRNA for P protein, and of RNase P for pre-tRNAAsp, overview
physiological function
additional information
evolution
-
the enzyme is conserved in all domains of life. The composition of RNase P varies from bacteria to archaea and eukarya, evolutionary enzyme spread, overview
evolution
-
two architectural subtypes of bacterial P RNAs, the phylogenetically prevailing ancestral type A represented by Escherichia coli P RNA, and Bacillus type B essentially confined to the low G + C Gram-positive bacteria, the prototype being Bacillus subtilis P RNA
physiological function
-
the RNase P holoenzyme is composed of a single RNA (type B1 RNase P RNA) and a single small protein subunit. Bacterial RNase P RNAs are comprised of two independently evolving domains, separated by P7. The RNA upstream and downstream of P7 contains all of the essential catalytic sequences and structures (C-domain). Changes in the RNA bound at each end by the two strands of P7 (the loop of P7) alter substrate specificity (S-domain). The RNA subunit is associated with a single, small conservative protein, encoded by the rnpA gene, which has an unusual left-handed betaalphabeta crossover connection and a large central cleft
physiological function
-
Bacillus subtilis RNase P, composed of a catalytically active RNA, PRNA, and a small protein, the P protein, subunit, catalyzes the 5' end maturation of precursor tRNAs. Inner-sphere coordination of divalent metal ions to PRNA is essential for catalytic activity, but not for the formation of the RNase P/pre-tRNA complex. Previous studies have demonstrated that this RNase P/pre-tRNA complex undergoes an essential conformational change before the cleavage step. The RNase P/pre-tRNA conformer is stabilized by a high affinity divalent cation capable of inner-sphere coordination, such as Ca2+ or Mg2+. A second, lower affinity Mg2+ activates cleavage catalyzed by RNase P. Conformational changes and structural analysis, overview
physiological function
-
the RNR motif of RNase P protein interacts with both catalytic RNA PRNA and pre-tRNA to stabilize an active conformer
physiological function
-
ribonuclease P catalyzes the metal-dependent 5' end maturation of precursor tRNAs
physiological function
-
the enzyme catalyzes the 5' end maturation of precursor tRNAs
physiological function
-
the enzyme catalyzes the maturation of the 5' end of precursor-tRNAs
physiological function
-
the principle task of the ubiquitous enzyme RNase P is the generation of mature tRNA 5'-ends by removing precursor sequences from tRNA primary transcripts
additional information
-
in bacteria, RNase P is composed of a catalytic RNA, PRNA, and a protein subunit, P protein, necessary for function in vivo. The P protein enhances pre-tRNA affinity, selectivity, and cleavage efficiency, as well as modulates the cation requirement for RNase P function. The RNR motif enhances a metal-stabilized conformational change in RNase P that accompanies substrate binding and is essential for efficient catalysis
additional information
-
in bacteria, RNase P is composed of a catalytic RNA and a protein subunit (P protein) necessary for function in vivo. The P protein enhances pre-tRNA affinity, selectivity, and cleavage efficiency, as well as modulates the cation requirement for RNase P function. The two residues R60 and R62 in the most highly conserved region of the P protein, the RNR motif formed by residues R60-R68, stabilize PRNA complexes with both P protein and pre-tRNA, overview. The RNR motif enhances a metal-stabilized conformational change in RNase P that accompanies substrate binding and is essential for efficient catalysis
additional information
-
in bacteria, the enzyme is a ribonucleoprotein composed of two essential subunits: a catalytic RNA subunit and a single small protein cofactor, P protein, secondary structure and tertiary interactions, overview. The RNA subunit of bacterial RNase P is an efficient catalyst in vitro in the absence of its single protein cofactor, while the protein cofactor is essential for RNase P function in vivo, affecting the structure, function, and kinetics of the holoenzyme under physiological salt conditions. In vitro, the protein subunit is dispensable, but its absence has to be compensated for by increased mono- and particularly divalent cations in order to achieve efficient RNA-alone catalysis
additional information
-
the metal-dependent conformational change re-organizes the bound substrate in the active site to form a catalytically competent RNase P-pre-tRNA complex
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
x * 13990-14000, protein subunit, + x * ?, RNA subunit, SDS-PAGE and mass spectrometry
additional information
additional information
-
RNA and protein subunits from one species can complement subunits from the other species in reconstitution experiments
additional information
-
the protein component both alters the conformation of the RNA component and enhances the substrate affinity and specificity
additional information
-
enzyme is composed of 1 RNA subunit of 350-450 nucleotides and 1 protein subunit of about 120 amino acids, the RNA subunit is divided into the specificity and the catalytic domain, i.e. S domain, comprising nucleotides 86-239, and C domain, comprising the rest of the molecule, overall and secondary structure, modeling
additional information
-
enzyme is composed of a large RNA subunit of about 400 nucleotides, and a small protein subunit of about 100 amino acids, global structure of the enzyme-substrate complex
additional information
-
primary and secondary structure of the ribozymal RNA, catalytic domain and specificity domain, structure of the ribozyme plays an important role in catalysis, overview
additional information
-
protein subunit structure, the enzyme folds as an alpha-beta sandwich and has the overall topology of alpha(beta)3alphabetaalpha, tertiary structure, overview
additional information
-
subunit composition, 1 large RNA subunit plus 1 small protein subunit contributing to about 10% of the mass of the holoenzyme
additional information
-
protein component influences holoenzyme dimer formation. Protein component does not stabilize the global structure of RNase P RNA. Differences between the two types of holoenzymes of Escherichia coli and Bacillus subtilis reside primarily in the RNA and not the protein components of each
additional information
-
Bacterial RNase P is composed of one RNA (PRNA, ca. 400 nucleotides [nt]) and one small protein subunit (P protein, ca. 120 amino acids)
additional information
-
in bacteria, RNase P is composed of a catalytic RNA, PRNA, and a protein subunit, P protein, necessary for function in vivo. The P protein enhances pre-tRNA affinity, selectivity, and cleavage efficiency, as well as modulates the cation requirement for RNase P function. Two residues, R60 and R62, in the most highly conserved region of the P protein, the RNR motif, R60-R68, stabilize PRNA complexes with both P protein and pre-tRNA. The RNR motif enhances a metal-stabilized conformational change in RNase P that accompanies substrate binding and is essential for efficient catalysis. Stabilization of this conformational change contributes to both the decreased metal requirement and the enhanced substrate recognition of the RNase P holoenzyme, illuminating the role of the most highly conserved region of P protein in the RNase P reaction pathway
additional information
-
enzyme secondary structure and tertiary interactions, overview
additional information
-
ribonuclease P is composed of a catalytically active RNA (PRNA) and a small protein (P protein) subunit
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ribonucleoprotein
ribonucleoprotein
-
the M1 RNA component is essential for the function of the enzyme
ribonucleoprotein
-
generation and characterization of circular Bacillus subtilis RNase P RNA. Activation by RNase P protein
ribonucleoprotein
-
the active site resides within the RNA moiety. The protein has a role in electrostatic shielding and aids in an essential conformational change
ribonucleoprotein
-
the enzyme requires an RNA as well as a protein subunit for its in vivo activity
ribonucleoprotein
-
the RNA moiety can cleave tRNA precursor molecules in buffer containing either 60 mM Mg2+ or 10 mM Mg2+ plus 1 mM spermidine. Under these conditions the protein moiety of the enzymes alone shows no catalytic activity
ribonucleoprotein
-
type B enzyme is a ribonucleoprotein and contains a single protein subunit
ribonucleoprotein
-
ribonuclease P is composed of a catalytically active RNA (PRNA) and a small protein (P protein) subunit
ribonucleoprotein
-
the enzyme is a ribonucleoprotein composed of two essential subunits: a catalytic RNA subunit (P RNA, 350-400 nt) and a single small protein cofactor, P protein, secondary structure and tertiary interactions, overview. The RNA subunit of bacterial RNase P is an efficient catalyst in vitro in the absence of its single protein cofactor, while the protein cofactor is essential for RNase P function in vivo, affecting the structure, function, and kinetics of the holoenzyme under physiological salt conditions
ribonucleoprotein
-
the enzyme is composed of a catalytic RNA (PRNA) and a protein subunit (P protein)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization of the S domain of the RNA subunit, X-ray diffraction structure determination and analysis at 3.15 A resolution, structure modeling
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E40C
-
site-directed mutagenesis, comparison of metal effects on enzyme-substrate complex formation with the wild-type enzyme
F16A
-
affinity of RNase P for A(-4) pre-tRNA is decreased more than 10fold
F20A
-
decrease in the affinity of A(-4) pre-tRNA compared to that of G(-4) pre-tRNA, causing the A(-4)/G(-4) selectivity ratio to decrease to less than 1. Mutations in the central cleft of P protein alters the observed cleavage rate constant by less than 2fold
K64C
R60A
R62A
R65A
R65C
R68A
R68C
Y113C
-
site-directed mutagenesis, comparison of metal effects on enzyme-substrate complex formation with the wild-type enzyme
Y34A
-
decrease in the affinity of A(-4) pre-tRNA compared to that of G(-4) pre-tRNA, causing the A(-4)/G(-4) selectivity ratio to decrease to less than 1. Mutations in the central cleft of P protein alters the observed cleavage rate constant by less than 2fold
Y34F
-
decreases A(-4) pre-tRNA binding affinity, although to a smaller extent than mutant Y34A. Binds A(-4) and P(-4) pre-tRNAs with comparable affinities. Mutations in the central cleft of P protein alters the observed cleavage rate constant by less than 2fold
additional information
K64C
-
site-directed mutagenesis of the RNR motif of P protein subunit, the mutant shows unaltered RNA binding kinetics compared to the wild-type enzyme
K64C
-
site-directed mutagenesis of an RNR motif residue, the mutant shows altered binding affinity for the substrate and between its components compared to the wild-type enzyme
R60A
-
decrease in the affinity of A(-4) pre-tRNA compared to that of G(-4) pre-tRNA, causing the A(-4)/G(-4) selectivity ratio to decrease to less than 1
R60A
-
site-directed mutagenesis of the RNR motif of P protein subunit, the mutant shows unaltered RNA binding kinetics compared to the wild-type enzyme
R60A
-
site-directed mutagenesis of an RNR motif residue, the mutant shows altered binding affinity for the substrate and between its components compared to the wild-type enzyme
R62A
-
site-directed mutagenesis of the RNR motif of P protein subunit, the mutant shows unaltered RNA binding kinetics compared to the wild-type enzyme
R62A
-
site-directed mutagenesis of an RNR motif residue, the mutant shows altered binding affinity for the substrate and between its components compared to the wild-type enzyme
R65A
-
affinity of RNase P for A(-4) pre-tRNA is decreased more than 10fold
R65A
-
site-directed mutagenesis of the RNR motif of P protein subunit, the mutant shows unaltered RNA binding kinetics compared to the wild-type enzyme
R65A
-
site-directed mutagenesis of an RNR motif residue, the mutant shows altered binding affinity for the substrate and between its components compared to the wild-type enzyme
R65C
-
site-directed mutagenesis of the RNR motif of P protein subunit, the mutant shows unaltered RNA binding kinetics compared to the wild-type enzyme
R65C
-
site-directed mutagenesis of an RNR motif residue, the mutant shows altered binding affinity for the substrate and between its components compared to the wild-type enzyme
R68A
-
site-directed mutagenesis of the RNR motif of P protein subunit, the mutant shows unaltered RNA binding kinetics compared to the wild-type enzyme
R68A
-
site-directed mutagenesis of an RNR motif residue, the mutant shows altered binding affinity for the substrate and between its components compared to the wild-type enzyme
R68C
-
site-directed mutagenesis of the RNR motif of P protein subunit, the mutant shows unaltered RNA binding kinetics compared to the wild-type enzyme
R68C
-
site-directed mutagenesis of an RNR motif residue, the mutant shows altered binding affinity for the substrate and between its components compared to the wild-type enzyme
additional information
-
construction of mutant enzyme chimeras consisting of either Escherichia coli protein components and Bacillus subtilis RNA component or vice versa
additional information
-
mutagenesis of the CR-IV region of the enzyme RPR1 RNA results in large reduction of kcat with little effect on Km
additional information
-
RNR motif mutations do not alter the kinetics of pre-tRNA cleavage
additional information
-
L5.1-L15.1 intradomain contact in the catalytic domain of the prototypic type B RNase P RNA of Bacillus subtilis is crucial for adopting a compact functional conformation. Disruption of the L5.1-L15.1 contact by antisense oligonucleotides or mutation reduces P RNA-alone and holoenzyme activity by one to two orders of magnitude in vitro, largely retards gel mobility of the RNA and further affects the structure of regions P7/P8/P10.1, P15 and L15.2, and abolishes the ability of Bacillus subtilis P RNA to complement a P RNA-deficient Escherichia coli strain
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
circular dichroism thermal denaturation studies of P protein (noncatalytic component of ribonuclease P) in the presence of stabilizing solute (osmolyte or ligand) to obtain a thermodynamic description of temperature-induced unfolding of the ligand-folded and trimethylamine N-oxide-folded conformations of P protein
additional information
-
circular dichroism thermal denaturation studies of P protein (noncatalytic component of ribonuclease P) in the presence of stabilizing solute (osmolyte or ligand) to obtain a thermodynamic description of temperature-induced unfolding of the ligand-folded and trimethylamine N-oxide-folded conformations of P protein
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
P protein purified by ion exchange chromatography under denaturing conditions
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
construction of a Bacillus subtilis mutant strain that conditionally expresses the RNase P protein under control of the xylose promoter (Pxyl)
-
expression of wild-type enzyme by in vitro transcription, expression of His-tagged enzyme
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
renaturation conditions for nearly 95% uniformly folded populations of enzyme or RNA substrate are: heating to 95°C for 3 min without divalent cation, cooling to 37°C and incubation in the presence of divalent cation for at least 15 min
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
medicine
-
RNase P RNA is a drug target for aminoglycoside-arginine conjugates
synthesis
-
the bacterial RNase P ribozyme might be used to release RNAs of interest with homogeneous 3'-OH ends from primary transcripts via site-specific cleavage, overview. Also, T7 transcription of mature tRNAs with clustered G residues at the 5'-end may result in 5'-end heterogeneities, which can be avoided by first transcribing the 5'-precursor tRNA (ptRNA) followed by P RNA-catalyzed processing to release the mature tRNA carrying a homogeneous 5'-monophosphate end
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cech, T.R.; Bass, B.L.
Biological catalysis by RNA
Annu. Rev. Biochem.
55
599-629
1986
Bacillus subtilis, Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
Pace, N.R.; Smith, D.
Ribonuclease P: function and variation
J. Biol. Chem.
265
3587-3590
1990
Bacillus subtilis, Saccharomyces cerevisiae, Homo sapiens, Schizosaccharomyces pombe, Xenopus laevis
James, B.D.; Olsen, G.J.; Liu, J.; Pace, N.R.
The secondary structure of ribonuclease P RNA, the catalytic element of a ribonucleoprotein enzyme
Cell
52
19-26
1988
Geobacillus stearothermophilus, Brevibacillus brevis, Priestia megaterium, Bacillus subtilis, Escherichia coli, Pseudomonas fluorescens
Reich, C.; Gardiner, K.J.; Olsen, G.J.; Pace, B.; Marsh, T.L.; Pace, N.P.
The RNA component of the Bacillus subtilis RNase P. Sequence, activity, and partial secondary structure
J. Biol. Chem.
261
7888-7893
1986
Bacillus subtilis
Gardiner, K.J.; Marsh, T.L.; Pace, N.R.
Ion dependence of the Bacillus subtilis RNase P reaction
J. Biol. Chem.
260
5415-5419
1985
Bacillus subtilis
Guerrier-Takada, C.; Gardiner, K.; Marsh, T.; Pace, N.; Altman, S.
The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme
Cell
35
849-857
1983
Bacillus subtilis, Escherichia coli
Gardiner, K.; Pace, N.R.
RNase P of Bacillus subtilis has a RNA component
J. Biol. Chem.
255
7507-7509
1980
Bacillus subtilis
Puttaraju, M.; Beebe, J.A.; Niranjanakumari, S.; Been, M.D.; Fierke, C.A.
Generation and characterization of circular Bacillus subtilis RNase P RNA; activation by RNase P protein
Nucleic Acids Symp. Ser.
33
92-94
1995
Bacillus subtilis
Niranjanakumari, S.; Kurz, J.C.; Fierke, C.A.
Expression, purification and characterization of the recombinant ribonuclease P protein component from Bacillus subtilis
Nucleic Acids Res.
26
3090-3096
1998
Bacillus subtilis
Xiao, S.; Scott, F.; Fierke, C.A.; Engelke, D.R.
Eukaryotic ribonuclease P: a plurality of ribonucleoprotein enzymes
Annu. Rev. Biochem.
71
165-189
2002
Bacillus subtilis, Saccharomyces cerevisiae, Cyanophora paradoxa, Escherichia coli, Homo sapiens, Methanothermobacter thermautotrophicus, Nicotiana tabacum, Spinacia oleracea
Ando, T.; Tanaka, T.; Kikuchi, Y.
Comparative analyses of hairpin substrate recognition by Escherichia coli and Bacillus subtilis ribonuclease P ribozymes
Biosci. Biotechnol. Biochem.
67
1825-1827
2003
Bacillus subtilis, Escherichia coli
Kurz, J.C.; Fierke, C.A.
Ribonuclease P: a ribonucleoprotein enzyme
Curr. Opin. Chem. Biol.
4
553-558
2000
Bacillus subtilis, Escherichia coli, Staphylococcus aureus
Harris, M.E.; Christian, E.L.
Recent insights into the structure and function of the ribonucleoprotein enzyme ribonuclease P
Curr. Opin. Struct. Biol.
13
325-333
2003
Bacillus subtilis, Escherichia coli
Gopalan, V.; Vioque, A.; Altman, S.
RNase P: variations and uses
J. Biol. Chem.
277
6759-6762
2002
Aspergillus nidulans, Bacillus subtilis, Saccharomyces cerevisiae, Cyanophora paradoxa, Escherichia coli, Homo sapiens, Leishmania sp., Mus musculus, Trypanosoma sp.
Xiao, S.; Houser-Scott, F.; Engelke, D.R.
Eukaryotic ribonuclease P: increased complexity to cope with the nuclear pre-tRNA pathway
J. Cell. Physiol.
187
11-20
2001
Bacillus subtilis, Bacteria, Saccharomyces cerevisiae, Cyanophora paradoxa, Homo sapiens, Spinacia oleracea
Christian, E.L.; Zahler, N.H.; Kaye, N.M.; Harris, M.E.
Analysis of substrate recognition by the ribonucleoprotein endonuclease RNase P
Methods
28
307-322
2002
Bacillus subtilis, Escherichia coli, Staphylococcus aureus
Hansen, A.; Pfeiffer, T.; Zuleeg, T.; Limmer, S.; Ciesiolka, J.; Feltens, R.; Hartmann, R.K.
Exploring the minimal substrate requirements for trans-cleavage by RNase P holoenzymes from Escherichia coli and Bacillus subtilis
Mol. Microbiol.
41
131-143
2001
Bacillus subtilis, Escherichia coli
Krasilnikov, A.S.; Yang, X.; Pan, T.; Mondragon, A.
Crystal structure of the specificity domain of ribonuclease P
Nature
421
760-764
2003
Bacillus subtilis
Henkels, C.H.; Oas, T.G.
Thermodynamic characterization of the osmolyte- and ligand-folded states of Bacillus subtilis ribonuclease P protein
Biochemistry
44
13014-13026
2005
Bacillus subtilis (P25814), Bacillus subtilis
Rueda, D.; Hsieh, J.; Day-Storms, J.J.; Fierke, C.A.; Walter, N.G.
The 5' leader of precursor tRNAAsp bound to the Bacillus subtilis RNase P holoenzyme has an extended conformation
Biochemistry
44
16130-16139
2005
Bacillus subtilis
Buck, A.H.; Dalby, A.B.; Poole, A.W.; Kazantsev, A.V.; Pace, N.R.
Protein activation of a ribozyme: the role of bacterial RNase P protein
EMBO J.
24
3360-3368
2005
Bacillus subtilis, Escherichia coli
Goessringer, M.; Kretschmer-Kazemi Far, R.; Hartmann, R.K.
Analysis of RNase P protein (rnpA) expression in Bacillus subtilis utilizing strains with suppressible rnpA expression
J. Bacteriol.
188
6816-6823
2006
Bacillus subtilis
Wegscheid, B.; Hartmann, R.K.
In vivo and in vitro investigation of bacterial type B RNase P interaction with tRNA 3-CCA
Nucleic Acids Res.
35
2060-2073
2007
Bacillus subtilis
Niranjanakumari, S.; Day-Storms, J.J.; Ahmed, M.; Hsieh, J.; Zahler, N.H.; Venters, R.A.; Fierke, C.A.
Probing the architecture of the B. subtilis RNase P holoenzyme active site by cross-linking and affinity cleavage
RNA
13
521-535
2007
Bacillus subtilis
Berchanski, A.; Lapidot, A.
Bacterial RNase P RNA is a drug target for aminoglycoside-arginine conjugates
Bioconjug. Chem.
19
1896-1906
2008
Bacillus subtilis
Kirsebom, L.A.; Trobro, S.
RNase P RNA-mediated cleavage
IUBMB Life
61
189-200
2009
Bacillus subtilis, Chlamydia sp., Homo sapiens, no activity in Nanoarchaeum equitans
Seif, E.; Altman, S.
RNase P cleaves the adenine riboswitch and stabilizes pbuE mRNA in Bacillus subtilis
RNA
14
1237-1243
2008
Bacillus subtilis, Bacillus subtilis 168
Koutmou, K.S.; Zahler, N.H.; Kurz, J.C.; Campbell, F.E.; Harris, M.E.; Fierke, C.A.
Protein-precursor tRNA contact leads to sequence-specific recognition of 5 leaders by bacterial ribonuclease P
J. Mol. Biol.
396
195-208
2010
Bacillus subtilis, Escherichia coli
McClain, W.H.; Lai, L.B.; Gopalan, V.
Trials, travails and triumphs: an account of RNA catalysis in RNase P
J. Mol. Biol.
397
627-646
2010
Geobacillus stearothermophilus, Bacillus subtilis, Escherichia coli, Mycoplasma genitalium, Salmonella enterica subsp. enterica serovar Typhimurium, Thermotoga maritima, no activity in Nanoarchaeum equitans
Cuzic-Feltens, S.; Weber, M.H.; Hartmann, R.K.
Investigation of catalysis by bacterial RNase P via LNA and other modifications at the scissile phosphodiester
Nucleic Acids Res.
37
7638-7653
2009
Bacillus subtilis, Escherichia coli
Koutmou, K.S.; Casiano-Negroni, A.; Getz, M.M.; Pazicni, S.; Andrews, A.J.; Penner-Hahn, J.E.; Al-Hashimi, H.M.; Fierke, C.A.
NMR and XAS reveal an inner-sphere metal binding site in the P4 helix of the metallo-ribozyme ribonuclease P
Proc. Natl. Acad. Sci. USA
107
2479-2484
2010
Bacillus subtilis
Ellis, J.; Brown, J.
The RNase P family
RNA Biol.
6
362-369
2009
Cupriavidus necator, Bacillus subtilis, Saccharomyces cerevisiae, Chlamydia trachomatis, Chlorobium limicola, Escherichia coli, Giardia intestinalis, Homo sapiens, Methanothermobacter thermautotrophicus, Methanocaldococcus jannaschii, Mycoplasmopsis fermentans, Mycoplasma hyopneumoniae, no activity in Aquifex aeolicus, Pyrobaculum aerophilum, Thermomicrobium roseum, Porphyra purpurea, Synechococcus elongatus PCC 6301, Reclinomonas americana
Hsieh, J.; Fierke, C.A.
Conformational change in the Bacillus subtilis RNase P holoenzyme-pre-tRNA complex enhances substrate affinity and limits cleavage rate
RNA
15
1565-1577
2009
Bacillus subtilis
Hsieh, J.; Koutmou, K.S.; Rueda, D.; Koutmos, M.; Walter, N.G.; Fierke, C.A.
A divalent cation stabilizes the active conformation of the B. subtilis RNase P x pre-tRNA complex: a role for an inner-sphere metal ion in RNase P
J. Mol. Biol.
400
38-51
2010
Bacillus subtilis
Koutmou, K.S.; Day-Storms, J.J.; Fierke, C.A.
The RNR motif of B. subtilis RNase P protein interacts with both PRNA and pre-tRNA to stabilize an active conformer
RNA
17
1225-1235
2011
Bacillus subtilis
Goessringer, M.; Helmecke, D.; Hartmann, R.K.
Characterization of RNase P RNA activity
Methods Mol. Biol.
848
61-72
2012
Aquifex aeolicus, Bacillus subtilis, Escherichia coli, Thermus thermophilus
Howard, M.J.; Liu, X.; Lim, W.H.; Klemm, B.P.; Fierke, C.A.; Koutmos, M.; Engelke, D.R.
RNase P enzymes: divergent scaffolds for a conserved biological reaction
RNA Biol.
10
909-914
2013
Bacillus subtilis, Saccharomyces cerevisiae, Homo sapiens, Thermotoga maritima, Trypanosoma brucei, Ostreococcus tauri, Arabidopsis thaliana (Q66GI4), Arabidopsis thaliana
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