Information on EC 3.1.26.5 - ribonuclease P

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
3.1.26.5
-
RECOMMENDED NAME
GeneOntology No.
ribonuclease P
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
show the reaction diagram
-
-
-
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
show the reaction diagram
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
show the reaction diagram
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, amino acids residues Arg90, Arg107, Lys123, Arg176, and Lys196 are involved in interaction with enzyme RNA or with the pre-tRNA
O59543
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
show the reaction diagram
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, chloroplast enzyme does not use the ribozyme-type pre-tRNA cleavage mechanism, distinct from bacterial reaction mechanism
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
show the reaction diagram
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
show the reaction diagram
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, conserved residues in J5/15 are responsible for substrate affinity and specificity of the ribozyme, nucleotide base N(-1) is involved in substrate recognition in bacteria and archea
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
show the reaction diagram
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, non-RNA-based cleavage mechanism, structure-function relationship of eukaryotic enzymes
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
show the reaction diagram
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, reaction mechanism in 3 consecutive steps: pre-tRNA binding, hydrolysis of the scissile phosphodiester bond, generating a 3'-hydroxyl and a 5'-phosphate group, possibly via a trigonal bipyramide, intermediate, and the dissociation of the mature tRNA and the 5'-leader product, structure-function relationship of eukaryotic enzymes
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
show the reaction diagram
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, reaction mechanism in 3 consecutive steps: pre-tRNA binding, hydrolysis of the scissile phosphodiester bond, generating a 3'-hydroxyl and a 5'-phosphate group, possibly via a trigonal bipyramide, intermediate, and the dissociation of the mature tRNA and the 5'-leader product, substrate recognition mechanism, overview, structure-function realtionship of eukaryotic enzymes
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
show the reaction diagram
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, RNA-based catalytic mechanism
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
show the reaction diagram
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, secondary structural features, e.g. helix P4, sequence J5/15 or J18/2 in the RNA portion of the enzyme, are important for catalysis
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, the RNA subunit is essential for catalytic activity, except for the mitochondrial enzyme, divalent metal ion-dependent in-line SN2 displacement mechanism
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
show the reaction diagram
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, the RNA subunit is the catalytic unit, while protein subunit Rpp25 is involved in RNA substrate binding, both interact with each other
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
show the reaction diagram
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, tRNA precursor substrate recognition and cleavage mechanism
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
show the reaction diagram
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
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
show the reaction diagram
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 important for tRNA binding
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
show the reaction diagram
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, tRNA precursor substrate recognition and cleavage mechanism, structure-function relationship of the RNA subunit
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
hydrolysis of phosphoric ester
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
tRNA processing
-
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aRpp29
O28362
-
aRpp29 protein
O28362
-
AtPop1p
L0N807
-
C5 protein
-
-
hPOP1
-
-
-
-
hPOP4
-
-
-
-
hPOP7
-
-
-
-
M1GS
synthetic construct
-
-
M1GS RNA
-
functional RNase P ribozyme
mitochondrial RNase P protein 1
-
-
nuclear ribonclease P ribonucleoprotein
-
-
nuclease, ribo-, P
-
-
-
-
Pfu Pop5
-
RNase P protein
PhoPRNA
Pyrococcus horikoshii OT-3
-
;
-
POP1
-
-
Pop1p
L0N807
-
PRORP
Q66GI4
-
PRORP1
-
gene name
PRORP2
-
gene name
Protein C5
-
-
-
-
Protein C5
-
-
proteinaceous RNase P
-
-
proteinaceous RNase P
Q66GI4
-
proteinaceous RNase P
-
-
proteinaceous RNase P
-
-
ribonuclease MRP
-
-
ribonuclease P
-
-
-
-
ribonuclease P
-
-
ribonuclease P
-
RNase P type B
ribonuclease P
-
RNase P
ribonuclease P
Escherichia coli MG1693
-
-
-
ribonuclease P
-
-
ribonuclease P
-
-
ribonuclease P
-
-
ribonuclease P
-
-
ribonuclease P
-
-
ribonuclease P
-
-
ribonuclease P
-
-
ribonuclease P
-
-
ribonuclease P
-
-
ribonuclease P
-
-
ribonuclease P
Pyrococcus horikoshii OT-3
-
;
-
ribonuclease P
-
-
ribonuclease P
-
-
ribonuclease P
-
RNase P
ribonuclease P
-
-
ribonuclease P
-
-
ribonuclease P
-
-
ribonuclease P
synthetic construct
-
-
ribonuclease P
-
-
ribonuclease P
-
-
ribonuclease P
-
-
ribonuclease P ribozyme
-
-
ribonuclease P ribozyme
-
-
ribosomal RNA processing ribonucleoprotein
-
-
Ribunuclease P
-
RNase 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
L0N807
-
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
RNase P
Bacillus subtilis 1A40
-
-
-
RNase P
-
-
RNase P
-
-
RNase P
-
RNase P RNA lacks the P15-loop structure but is still capable to mediate cleavage at the canonical RNase P cleavage site
RNase P
Clostridium innocuum
-
-
RNase P
-
consists of a catalytic RNA subunit (M1 RNA) and a protein component (C5 protein)
RNase P
-
the bacterial RNase P comprises an RNA subunit and a small protein subunit
RNase P
Escherichia coli MG1693
-
;
-
RNase P
-
human mitochondrial RNase P does not require a trans-acting RNA component for catalysis, the enzyme is composed of a tRNA methyltransferase, a short-chain dehydrogenase/reductase-family member, and a protein of hitherto unknown functional and evolutionary origin, possibly representing the enzyme's metallonuclease moiety
RNase P
-
the catalytic RNA subunit of RNase P is a trans-acting ribozyme that cleaves various RNA substrates in vitro generating 5'-phosphates and 3'-hydroxyls as cleavage products
RNase P
-
the human mitochondrial RNase P is an entirely protein-based enzyme
RNase P
-
-
RNase P
P43039
-
RNase P
P47703
-
RNase P
Q4A750
-
RNase P
Q6KH14
-
RNase P
Q6MRS3
-
RNase P
Q8EU90
-
RNase P
-
-
RNase P
P75111
-
RNase P
Q98R57
-
RNase P
Q4A5G4
-
RNase P
no activity in Nanoarchaeum equitans
-
-
RNase P
Q00XA5
-
RNase P
Ostreococcus tauri RCC745
Q00XA5
-
-
RNase P
Pyrobaculum sp.
-
-
RNase P
-
the catalytic RNA subunit RPR of ribonuclease P is associated with four protein subunits homologous to four eukaryotic nuclear RNase P proteins: RPP21, RPP29, RPP30, and POP5
RNase P
-
contains catalytic RNA and the RNase P proteins PhoRpp21 and PhoRpp29
RNase P
Pyrococcus horikoshii OT-3
-
;
-
RNase P
-
contains of the RNA subunit Rpr1r and the protein subunits Pop1p and Rpr1r
RNase P
-
yeast RNase P has a RNA component and nine protein components: Pop1, Pop3, Pop4, Pop5, Pop6, Pop7, Pop8, Rpp1, and Rpr2, all these proteins are essential for the activity of the enzyme in vivo
RNase P
-
yeast RNase P holoenzyme comprises one RNA subunit and nine protein subunits
RNase P
Saccharomyces cerevisiae SCWY10
-
yeast RNase P holoenzyme comprises one RNA subunit and nine protein subunits
-
RNase P
Saccharomyces cerevisiae YSW1
-
; yeast RNase P has a RNA component and nine protein components: Pop1, Pop3, Pop4, Pop5, Pop6, Pop7, Pop8, Rpp1, and Rpr2, all these proteins are essential for the activity of the enzyme in vivo
-
RNase P
-
-
RNase P
synthetic construct
-
-
RNase P
Q9X1H4
-
RNase P
-
-
RNase P
Q9PPN6
-
RNase P holoenzyme
-
-
RNase P protein
-
-
-
-
RNase P protein
-
-
RNase P protein
Q00XA5
-
RNase P protein
Ostreococcus tauri RCC745
Q00XA5
-
-
RNase P RNA
-
-
RNase P RNA
-
-
RNase P RNA
Pyrococcus horikoshii OT-3
-
-
-
RNase P RNA
-
-
RNase P/MRP
-
-
RNase P/MRP protein
L0N807
-
RNase P/MRP protein
-
-
RNase P/MRP protein
-
-
RNaseP protein
-
-
-
-
RNaseP protein p20
-
-
-
-
RNaseP protein p30
-
-
-
-
RNaseP protein p38
-
-
-
-
RNaseP protein p40
-
-
-
-
RPP
Q00XA5
-
RPP
Ostreococcus tauri RCC745
Q00XA5
-
-
Rpp21
-
-
Rpp29
-
-
Rpp38
-
-
RPP40
-
-
transfer RNA 5' maturation enzyme
-
-
transfer RNA processing enzyme
-
-
tRNA processing enzyme
-
-
tRNA processing enzyme
-
-
tRNA-processing endonuclease
-
-
tRNA-processing enzyme
-
-
CAS REGISTRY NUMBER
COMMENTARY
71427-00-4
not distinguished from EC 3.1.26.7
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Ajellomyces capsulatus
-
-
-
Manually annotated by BRENDA team
AtPop1p protein with RNase P activity
UniProt
Manually annotated by BRENDA team
enzyme is a catalytically active RNA with only a small additional protein subunit
-
-
Manually annotated by BRENDA team
gene rnpB, type B enzyme
-
-
Manually annotated by BRENDA team
strain 1A40
-
-
Manually annotated by BRENDA team
the B-type enzyme is a ribonucleoprotein
-
-
Manually annotated by BRENDA team
Bacillus subtilis 1A40
strain 1A40
-
-
Manually annotated by BRENDA team
enzyme is a catalytically active RNA, at least 2 isoforms with different substrate specificities
-
-
Manually annotated by BRENDA team
Clostridium innocuum
-
-
-
Manually annotated by BRENDA team
gene rnpA encodes C5 protein, gene mpB encodes the catalytic M1 RNA subunit
-
-
Manually annotated by BRENDA team
gene rnpB encoding the RNA subunit, gene rnpA encoding the protein subunit
-
-
Manually annotated by BRENDA team
gene rnpB, type A enzyme
-
-
Manually annotated by BRENDA team
strain MG1693
-
-
Manually annotated by BRENDA team
strain MRE600
-
-
Manually annotated by BRENDA team
the catalytic RNA component is encoded by the gene rnpB and the protein moiety by gene rnpA
-
-
Manually annotated by BRENDA team
wild-type strain and temperature-sensitive mutant that is defective in RNase P activity
-
-
Manually annotated by BRENDA team
wild-type strain and two temperature-sensitive mutant strains, ts241 and ts709
-
-
Manually annotated by BRENDA team
Escherichia coli MG1693
gene rnpA encodes C5 protein, gene mpB encodes the catalytic M1 RNA subunit
-
-
Manually annotated by BRENDA team
Escherichia coli MG1693
strain MG1693
-
-
Manually annotated by BRENDA team
Escherichia coli MRE600
strain MRE600
-
-
Manually annotated by BRENDA team
P62426: ribosomal protein L7Ae, P60780: subunit Pop5, P60781: subunit rnp3, P60832: subunit rnp1, P62378: subunit rnp4
P62426 and P60780 and P60781 and P60832 and P62378
SwissProt
Manually annotated by BRENDA team
formerly Methanobacterium thermoautotrophicum strain DELTAH, type A enzyme
-
-
Manually annotated by BRENDA team
ribonuclease P protein component
UniProt
Manually annotated by BRENDA team
ribonuclease P protein component
UniProt
Manually annotated by BRENDA team
ribonuclease P protein component
UniProt
Manually annotated by BRENDA team
ribonuclease P protein component
UniProt
Manually annotated by BRENDA team
ribonuclease P protein component; subspecies Mycoplasma mycoides mycoides SC
UniProt
Manually annotated by BRENDA team
ribonuclease P protein component
UniProt
Manually annotated by BRENDA team
ribonuclease P protein component
UniProt
Manually annotated by BRENDA team
ribonuclease P protein component
UniProt
Manually annotated by BRENDA team
ribonuclease P protein component
UniProt
Manually annotated by BRENDA team
no activity in Aquifex aeolicus
-
-
-
Manually annotated by BRENDA team
no activity in Nanoarchaeum equitans
-
-
-
Manually annotated by BRENDA team
component RNPA
UniProt
Manually annotated by BRENDA team
Ostreococcus tauri RCC745
component RNPA
UniProt
Manually annotated by BRENDA team
strain 3D7
-
-
Manually annotated by BRENDA team
Pyrobaculum sp.
-
-
-
Manually annotated by BRENDA team
strain OT3
Uniprot
Manually annotated by BRENDA team
Pyrococcus horikoshii OT-3
-
-
-
Manually annotated by BRENDA team
Pyrococcus horikoshii OT-3
strain OT3
Uniprot
Manually annotated by BRENDA team
Pyrococcus horikoshii OT-3
strain OT3
-
-
Manually annotated by BRENDA team
strain SCWY10
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae SCWY10
strain SCWY10
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae YSW1
-
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae YSW1
strain YSW1
-
-
Manually annotated by BRENDA team
strain PCC 6803
-
-
Manually annotated by BRENDA team
synthetic construct
-
-
-
Manually annotated by BRENDA team
enzyme is not a RNA-dependent ribozyme, but may contain an RNA component
-
-
Manually annotated by BRENDA team
genes PRORP1 and PRORP2
-
-
Manually annotated by BRENDA team
ribonuclease P protein component
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
Q00XA5
comparison of nuclear, mitochondrial, and plastidic RPPs, overview
evolution
-
Dictyostelium discoideum nuclear RNase P is a ribonucleoprotein complex that displays similarities with its counterparts from higher eukaryotes such as the human enzyme, but at the same time it retains distinctive characteristics
evolution
-
evolutionary history of PRORP, overview
evolution
Pyrobaculum sp.
-
identification in select archaea of an unusual archetype of the RNase P RNA
evolution
-
the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs
evolution
-
in the evolved, modern RNase P enzymes, the RNA depends on protein to fulfill its cellular function. This RNA-based form of RNase P is found in all domains of life, but there is an apparent trend from RNA to protein predominance in the overall composition and functioning of these ribonucleoproteins from bacteria to eukarya. RNase P of the former is built from a catalytically proficient RNA and a single small protein only. RNase P RNA of Archaea is a less-efficient catalyst in vitro and associates with five proteins, none of which is related to the bacterial protein. Another entirely different form of RNase P, i.e. proteinaceous RNase P, apparently not containing RNA, is initially observed in the organelles of different eukarya, e.g. humans, and also in Trypanosoma brucei. The genomes of trypanosomatids lack evidence for genes related to RNA-based RNase P, but they encode two homologues of human and plant PRORP genes. Also in plants, all cellular tRNA 5' end maturation appears to be exclusively protein dependent
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
-
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. The chloroplast and mitochondrial genomes of Ostreococcus tauri encode distinct individual RNase P RNA genes and the nucleus encodes both a bacterial-like RNase P protein component, and a proteinaceous RNase P enzyme
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. The protozoan Trypanosoma brucei harbors 2 PRORP isoforms, both of which have 5' pre-tRNA processing activity in vitro. One isoform (PRORP1) localizes to the nucleus and the second (PRORP2) to the mitochondrion
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
evolution
Ostreococcus tauri RCC745
-
comparison of nuclear, mitochondrial, and plastidic RPPs, overview
-
evolution
-
Dictyostelium discoideum nuclear RNase P is a ribonucleoprotein complex that displays similarities with its counterparts from higher eukaryotes such as the human enzyme, but at the same time it retains distinctive characteristics
-
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
malfunction
-
in a strain carrying the rnpA49 allele, encoding temperature sensitive RNase P, thermal inactivation of RNase P leads to ca. 60% reduction in relative quantities of the mature tRNA, although there is no change the relative quantities of the primary transcripts. Inactivation of both RNase P and RNase E leads to disappearance of the majority of the heterogeneous pre-tRNA precursor species except for the species containing the intact 5'-end and a processed 3'-end. In the absence of RNase P (both rnpA49 and rnpA49 rne-1) ca. 77% (36/49) of the transcripts have immature 3' termini containing 1-3 nt downstream of the CCA
malfunction
-
in both deletion mutants Rpp20(16-140) and Rpp20(35-140) the global thermodynamics of the interaction with Rpp25 is seemingly unaffected. Thermodynamic signature of the association is also fully preserved between the Rpp25(25-170) mutant and all available versions of Rpp20. Regions within the mutants Rpp20(35-140) and Rpp25(25-170) are sufficient for mutual interaction, thus this recognition can be mediated largely, if not exclusively, by the Alba-type core domains
malfunction
-
inactivation of RNase P results in decreased transcription of several non-coding RNAs in a cell cycle-dependent fashion
malfunction
synthetic construct
-
mutant M1-C2 is catalytically inactive
malfunction
-
absence of the enzyme in mutant rnpA49 rph-1 strain results in accumulation of unprocessed large tRNA transcripts and a 4fold decrease in mature species
malfunction
-
deletion of the S-domain reduces the activity rate, changes the Mg2+ requirement, and has a significant impact on the kinetic of cleavage for substrates carrying C-1/G+73. Substitutions in the truncated mutant, e.g. at pposition 248, can partly compensate for the absence of the S-domain, overview
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
-
an in vitro transcribed RNase P RNA is catalytically active
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
physiological function
-
binding of RPP29 to RPP21 involves binding-coupled folding and stabilization of interfacial structures in RPP29. When bound to its partner, RPP21 adopts the same overall L-shaped structure observed in the free protein: a long arm containing the two N-terminal alpha-helices, a short-arm made up of the C-terminal beta-sheet comprising the zinc ribbon, and a central linker connecting the two domains. In the complex, helix alpha1 of RPP21 extends through residues 9-17, indicating that binding is associated with induced fit in RPP21 as well. The N-terminal region of RPP29 extends in an antiparallel fashion along RPP21 helix alpha1. RPP29 beta2 interacts with both helices of RPP21 in the center of the interface, and the C-terminal helix of RPP29 stabilizes the end of RPP21 helix alpha2. The RPP21RPP29 complex is localized to the specificity domain of the RNase P RNA. Sm-like core of RPP29 is essentially unchanged by RPP21 binding
physiological function
-
Ignicoccus hospitalis is the host of Nanoarchaeum equitans, who has no RNase P and is dependent on its host RNase P activity for transfer of metabolites, energy and amino acids
physiological function
-
in the presence of the RPP29RPP21 complex, the paired regions P9, P10/11, and P12 in the S-domain are protected from V1 cleavage, while no protection by RPP29RPP21 complex is observed in the C-domain
physiological function
-
mitochondrial RNase P RNA is primitive and recognizably similar to those of alpha-proteobacteria, the ancestors of mitochondria
physiological function
-
native nuclear RNase P has an RNase P RNA plus nine RNase P proteins. All subunits are essential for RNase P activity and cell viability. Only the nuclear-encoded RPM2 is known and shown genetically to be required for mitochondrial RNase P activity
physiological function
-
native nuclear RNase P has an RNase P RNA plus ten RNase P proteins. The protein-only mitochondrial RNase P is composed of three proteins (MRPP1-MRPP3). MRPP1, which methylates G9 of tRNAs, may be responsible for substrate recognition. RNase P RNA is weakly active without RNase P proteins, some activity is present when reconstituted with RPP21 and RPP29
physiological function
-
plastid RNase P RNA in the non-green alga is similar to those of their cyanobacterial ancestry
physiological function
-
RNase P is an essential enzyme that catalyzes the 5' endonucleolytic cleavage of pre-tRNAs. RNase MRP, a variant of RNase P that has evolved to participate in ribosomal RNA processing, is also involved in turnover of specific messenger RNAs. RNase P and RNase MRP have eight proteins in common, with the RNA subunits being related but diverged. RNase P has one distinctive protein subunit (Rpr2p), while RNase MRP has two (Snm1p, Rmp1p). Nuclear RNase P is involved in a pathway for alternative maturation of intron-encoded box C/D snoRNAs
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
physiological function
synthetic construct
-
Salmonella can efficiently deliver RNase P-based ribozyme sequence in specific human cells, leading to substantial ribozyme expression and effective inhibition of viral infection: targeted gene delivery of RNase P ribozyme by Salmonella to human cytomegalovirus-infected cells results in effective inhibition of viral gene expression and replication. Functional RNase P ribozyme (M1GS RNA) that targets the overlapping mRNA region of two human cytomegalovirus capsid proteins, the capsid scaffolding protein and assemblin, which are essential for viral capsid formation. A reduction of 87-90% in viral capsid scaffolding protein expression and a reduction of about 5000fold in viral growth in cells that are treated with Salmonella carrying the sequence of the functional ribozyme
physiological function
-
strong interaction between Rpp25 and Rpp20. Rpp20 and Rpp25 interact with the P3 arm of RNase MRP RNA in a highly synergic fashion. Rpp20 and Rpp25 interact with the P3 RNA as a heterodimer, which is formed prior to RNA binding. Association between Rpp20 and Rpp25 has no detectable influence on their secondary/tertiary structure. The association reaction results in a large loss of solvent-accessible area. N- and C-terminal regions of Rpp25 and the N-terminal tail of Rpp20 are not involved in mutual recognition
physiological function
-
the holoenzyme consists of a single RNase P RNA associated with RNase P protein subunits
physiological function
-
the mitochondrial RNase P is devoid of any RNA, mitochondria make their RNase P of three proteins only. MRPP1 is involved in the methylation of G9 in mitochondria in addition to its role in mitochondrial RNase P. MRRP2 may contribute RNA binding activity to mitochondrial RNase P via its conserved NAD+-binding domain. In its C-terminal half MRPP3 displays a handful of amino acid residues strictly conserved in their identity and spacing and reminiscent of a metallonuclease's active site: three aspartates and a histidine, the latter proposed to be directly involved in catalysis
physiological function
-
the nuclear holoenzyme is comprised of protein subunits and RNase P RNA. In mitochondria, the usual RNA-containing RNase P is replaced by an enzyme composed of three proteins that are unrelated to RNase P enzymes in other systems (Rube Goldberg triad of unrelated proteins), but nevertheless are together responsible for the cleavage of pre-tRNA precursors
physiological function
-
the organism has distinct RNase P enzymes in the nucleus and mitochondria. The RNase P RNA from the mitochondrion is an example of a highly-derived (degenerate) mitochondrial RNase P RNA
physiological function
-
the RNase P holoenzyme is composed of a single RNA (type A1 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
-
the RNase P holoenzyme is composed of a single RNA (type A2 RNase P RNA, lacks P13 and P14) 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
-
the RNase P holoenzyme is composed of a single RNA (type A3 RNase P RNA, with an altered L15 internal loop, in which the substrate 3'-NCCA tail is recognized) 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
-
the RNase P holoenzyme is composed of a single RNA (type A4 RNase P RNA, with an altered L15) 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
-
the RNase P holoenzyme is composed of a single RNA (type A5 RNase P RNA, lacks P18) 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
-
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
-
the RNase P holoenzyme is composed of a single RNA (type B2 RNase P RNA, lacks P10.1) 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
-
the RNase P holoenzyme is composed of a single RNA (type B3 RNase P RNA, lacks P12) 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
-
the RNase P holoenzyme is composed of a single RNA (type C 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
-
the RNase P holoenzyme is composed of a single RNA molecule (type A RNase P RNA) and several protein subunits
physiological function
-
the RNase P holoenzyme is composed of a single RNA molecule (type M RNase P RNA, lacking P6, P8, P16 and P17) and several protein subunits
physiological function
-
the RNase P holoenzyme is composed of a single RNA molecule (type T RNase P RNA, lacking the S-domain) and several protein subunits
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
-
nuclear RNase P is required for transcription and processing of tRNA
physiological function
Q00XA5
RNase P catalyzes 5'-maturation of tRNAs. Recombinant Ostreococcus tauri RPP can functionally reconstitute with bacterial RNase P RNAs but not with Ostreococcus tauri organellar RPRs, despite the latter's presumed bacterial origin
physiological function
-
RNase P is a catalytic ribonucleoprotein primarily involved in tRNA biogenesis. Insights into the role of protein cofactors RPPs in substrate recognition and cleavage-site selection. Cleavage of various model hairpin loop substrates in the presence of archaeal RPPs
physiological function
Pyrobaculum sp.
-
RNase P is a ubiquitous and essential endoribonuclease. It is a catalytic ribonucleoprotein complex that employs an RNA catalyst and Mg2+ ions to cleave precursor RNAs (pre-RNAs) and generate the 5' termini of mature RNAs such as tRNA, 4.5S RNA, tmRNA, and other cellular RNAs
physiological function
-
RNase P is an essential endoribonuclease processing the 59 leader of pre-tRNAs. Compared to bacterial RNase P, which contains a single small protein subunit and a large catalytic RNA subunit, eukaryotic nuclear RNase P is more complex, containing nine proteins and an RNA subunit in Saccharomyces cerevisiae. Nuclear RNase P has been shown to possess unique RNA binding capabilities, molecular recognition of nuclear RNase P, overview. Multiple interactions are required for high affinity binding
physiological function
-
RNase P is an essential endoribonuclease that catalyzes the cleavage of the 59 leader of pre-tRNAs. In addition, a growing number of non-tRNA substrates are identified in various organisms. RNase P varies in composition, as bacterial RNase P contains a catalytic RNA core and one protein subunit, while eukaryotic nuclear RNase P retains the catalytic RNA but has at least nine protein subunits. The additional eukaryotic protein subunits most likely provide additional functionality to RNase P, with one possibility being additional RNA recognition capabilities
physiological function
-
RNase P processes tRNAs by cleavage of precursor-tRNAs. RNase P is a ribozyme. The RNA component catalyzes tRNA maturation in vitro without proteins
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
-
the stem loops of the RNase P RNA are required as binding sites for the proteins, their interactions are predominantly involved in stabilizing the active conformation of the enzyme
physiological function
-
the ubiquitous endonuclease RNase P is responsible for the 5' maturation of tRNA precursors. In Arabidopsis thaliana mitochondria and plastids, a single protein called proteinaceous RNase P, PRORP1, can perform the endonucleolytic maturation of tRNA precursors that defines RNase P activity. In addition, PRORP1 is able to cleave tRNA-like structures involved in the maturation of plant mitochondrial mRNAs
physiological function
-
ribonuclease P is a ribonucleoprotein complex involved in the processing of the 5'-leader sequence of precursor tRNA (pre-tRNA). RNaseP proteins are predominantly involved in optimization of the pRNA conformation, though they are individually dispensable for RNase P activity in vitro
physiological function
-
the enzyme is involved in the procvessing of the leader sequence of precursor tRNA
physiological function
-
ribonuclease P catalyzes the metal-dependent 5' end maturation of precursor tRNAs
physiological function
-
RNase P is the endonuclease that removes 5' extensions from tRNA precursors, an early and essential step in tRNA biogenesis. PRORP1 Is able to substitute for Saccharomyces cerevisiae strain BY4743 nuclear RNase P in vivo, the inherently different physical qualities of the two enzyme forms are not reflected in a basically different functionality
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 enzyme catalyzes the maturation of the 5' end of precursor-tRNAs. Trypanosoma brucei proteinaceous enzyme PRORP1 can substitute for yeast nuclear RNase P in vivo. Proteinaceous PRORP1 catalyzes all of the other noncanonical, yet vital functions of nuclear yeast RNase P, which may include processing of non-canonical RNAs
physiological function
-
the enzyme catalyzes the Mg2+-dependent 5'-maturation of precursor tRNAs
physiological function
-
the enzyme catalyzes tRNA 5' maturation
physiological function
-
the enzyme is a ribonuleoprotein that catalyzes the processing of 5' leader sequences from tRNA precursors and other noncoding RNA in all living cells
physiological function
-
the enzyme is an essential ribonucleoprotein enzyme that is responsible for catalyzing the maturation of the 5' end of transfer RNAs through site-specific hydrolysis of a phosphodiester bond in precursor tRNAs. The single enzyme processes the 5' ends of tRNA precursors in cells and organelles that carry out tRNA biosynthesis. Rates of ptRNA processing by RNase P are tuned for uniform specificity and consequently optimal coupling to precursor biosynthesis
physiological function
Q9X1H4
the enzyme is an RNA-based enzyme primarily responsible for 5'-end pre-tRNA processing
physiological function
-
the enzyme is essential
physiological function
-
the enzyme is required for the initial separation of all seven valine tRNAs from three distinct polycistronic transcripts, the processing of the seven valine tRNAs in Escherichia coli demands special features of the enzyme. Processing of the valU polycistronic transcript is completely dependent on RNase P. Processing of the lysT polycistronic operon requires RNase P but is stimulated by RNase E, EC 3.1.26.12
physiological function
-
the enzyme RNase P is a tRNA processing enzyme. The enzyme can mediate inhibition of human cytomegalovirus gene expression and replication in U373MG cells, and the viral capsid formation, induced by engineered external guide sequences, overview. External guide sequences (EGSs) are RNA molecules that can bind to a target mRNA and direct ribonuclease P for specific cleavage of the target mRNA. Construction of EGS variants that efficiently direct human RNase P to cleave a target mRNA, coding for human cytomegalovirus capsid scaffolding protein and assemblin, in vitro. The EGS variant is about 40fold more active in directing human enzyme to cleave the mRNA in vitro than the EGS derived from a natural tRNA
physiological function
-
the mutant enzyme variant is more effective in HIV RNA sequence cleavage and reducing HIV-1 p24 expression and intracellular viral RNA level in cells than the wild-type ribozyme. A reduction of about 90% in viral RNA level and a reduction of 150fold in viral growth are observed in human H9 cells that express the mutant, while a reduction of less than 10% is observed in H9 cells that either do not express the ribozyme or produce a catalytically inactive ribozyme mutant
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
physiological function
-
the ribonucleoprotein endoribonuclease is responsible for 5' maturation of precursor tRNA
physiological function
Ostreococcus tauri RCC745
-
RNase P catalyzes 5'-maturation of tRNAs. Recombinant Ostreococcus tauri RPP can functionally reconstitute with bacterial RNase P RNAs but not with Ostreococcus tauri organellar RPRs, despite the latter's presumed bacterial origin
-
physiological function
Escherichia coli MG1693
-
the enzyme is required for the initial separation of all seven valine tRNAs from three distinct polycistronic transcripts, the processing of the seven valine tRNAs in Escherichia coli demands special features of the enzyme. Processing of the valU polycistronic transcript is completely dependent on RNase P. Processing of the lysT polycistronic operon requires RNase P but is stimulated by RNase E, EC 3.1.26.12
-
physiological function
Pyrococcus horikoshii OT-3
-
the stem loops of the RNase P RNA are required as binding sites for the proteins, their interactions are predominantly involved in stabilizing the active conformation of the enzyme
-
malfunction
Escherichia coli MG1693
-
in a strain carrying the rnpA49 allele, encoding temperature sensitive RNase P, thermal inactivation of RNase P leads to ca. 60% reduction in relative quantities of the mature tRNA, although there is no change the relative quantities of the primary transcripts. Inactivation of both RNase P and RNase E leads to disappearance of the majority of the heterogeneous pre-tRNA precursor species except for the species containing the intact 5'-end and a processed 3'-end. In the absence of RNase P (both rnpA49 and rnpA49 rne-1) ca. 77% (36/49) of the transcripts have immature 3' termini containing 1-3 nt downstream of the CCA, absence of the enzyme in mutant rnpA49 rph-1 strain results in accumulation of unprocessed large tRNA transcripts and a 4fold decrease in mature species
-
additional information
-
Arabidopsis thaliana PRORP1 can replace the bacterial ribonucleoprotein RNase P in Escherichia coli cells
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
-
RNas P RNA solution structure determination using small angle X-ray scattering and selective 29-hydroxyl acylation analyzed by primer extension, SHAPE, analysis, generation of all-atom RNA models, overview. Ab initio modeling fails to define unique scattering envelopes
additional information
-
the catalytic RNP has an H1 RNA moiety associated with ten distinct protein subunits. Five out of eight of these protein subunits, Rpp20, Rpp21, Rpp25, Rpp29, and Pop5, prepared in refolded recombinant forms, bind to H1 RNA in vitro. Rpp20 and Rpp25 bind jointly to H1 RNA, even though each protein can interact independently with this transcript. Nuclease footprinting analysis reveals that Rpp20 and Rpp25 recognize overlapping regions in the P2 and P3 domains of H1 RNA. Rpp21 and Rpp29, which are sufficient for reconstitution of the endonucleolytic activity, bind to separate regions in the catalytic domain of H1 RNA, subunit binding site analysis on H1 RNA, overview
additional information
Pyrobaculum sp.
-
the Pyrobaculum sp. RNase P RNA is about 50% smaller compared to other archaeal RNase Ps
additional information
-
all existing bacterial versions of the rnpA sequence might retain the elements required for functional interaction with the RNase P RNA. But the similarity of the heterologue to the endogenous version does not predict the fitness costs of the replacement
additional information
-
Arabidopsis thaliana contains a protein only form of RNase P, modeling of PRORP-tRNA interaction
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 (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. 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 effi cient RNA-alone 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
-
in plants, the protein Pop1p is associated with MRP RNAs, i.e. mitochondrial RNA processing RNAs which cleave the large rRNA precursor at the A3 site, and with the catalytic subunit of enzyme RNase P, either separately or in a single large complex. Pop1p-specific antibodies precipitate RNase P activity from wheat extracts. The eukaryotic RNase P consensus sequence with CR II and CR III that are signature elements specific for RNase P RNA
additional information
L0N807
in plants, the protein Pop1p is associated with MRP RNAs, i.e. mitochondrial RNA processing RNAs which cleave the large rRNA precursor at the A3 site, and with the catalytic subunit of enzyme RNase P, either separately or in a single large complex. The eukaryotic RNase P consensus sequence with CR II and CR III that are signature elements specific for RNase P RNA
additional information
-
modeling of RNP-based RNase P
additional information
-
RNase P-mediated inhibition of gene expression represents a novel and promising nucleic acid-based gene interference strategy for specific inhibition of target mRNA, overview
additional information
-
structure-function analysis of proteinaceous RNase P, i.e. the enzyme consisting of only a protein part without catalytic RNA. The anticodon domain of transfer RNA is dispensable, whereas individual residues in D and TpsiC loops are essential for enzyme function, enzyme/transfer RNA interaction, mode of action of the proteinaceous enzyme, overview. Transfer RNA recognition by the proteinaceous PRORP enzyme is similar to that by ribonucleoprotein RNase P enzyme
additional information
-
the enzyme is a ribonlucleoprotein, the RNAsubunit, termed P RNA, contains the active site, whereas the smaller protein subunit is required for optimal molecular recognition and catalysis in vitro and is essential in vivo
additional information
-
the enzyme is a ribonucleoprotein consisting of one protein and one RNA subunit, referred to as C5 and RNase P RNA, respectively. The RNase P RNA is composed of domains that have different functions, the structural architecture of the -1/+73 plays a significant role where a C-1/G+73 pair has the most dramatic effect on kobs
additional information
-
the enzyme is composed of RNA and five proteins (UniProtIDs: O59425, O59150, O59543, and O59248), the proteins assists the RNA part in attaining a functionally active conformation via a distinct mode of binding. Three archaeal proteins, PhoPop5, PhoRpp29, and PhoRpp30, are capable of promoting both, RNA annealing and displacement activities. They function as RNA chaperones or RNA annealers, fluorescence spectrometric analysis, overview. Protein PhoRpp21 shows low activity as annealer, and proein PhoRpp38 is inactive in annealing and strand displacement
additional information
-
the enzyme is composed of two proteins, which localize to the nucleus and the mitochondrion, respectively, and have RNase P activity each on their own. The proteins PRORP1 and PRORP2 are the sole forms of RNase P in trypanosomatids
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
additional information
-
the organellar RNase P RNAs are expressed in vivo, however under in vitro conditions, catalysis of pre-tRNA cleavage is not observed even when associated with the nuclear encoded bacterial-like protein. Modeling of PRORP-tRNA interaction and RNP-based RNase P
additional information
-
the two protein subunits StPop5 and StRpp25 are associated with with floral bud enzyme activity but not with leaf enzyme activity
additional information
Q9X1H4
wild-type and mutant enzyme structure-function analysis, overview. RNA U52 and two bacterially conserved protein residues, F17 and R89, are essential for efficient Thermotoga maritima enzyme activity. The U52 nucleotide binds a metal ion at the active site, whereas F17 and R89 are positioned over 20 A from the cleavage site, probably making contacts with N-4 and N-5 nucleotides of the pretRNA 5'-leader
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
10Sa RNA + H2O
?
show the reaction diagram
-
-
-
-
?
4.55 rRNA precursor + H2O
mature 4.55 rRNA + 5'-oligonucleotide
show the reaction diagram
-
-
-
-
?
4.5S RNA precursor + H2O
mature 4.5S RNA + 5'-oligonucleotide
show the reaction diagram
-
RNA processing
-
-
?
4.5S RNA, precursor to + H2O
?
show the reaction diagram
-
-
-
-
?
4.5S RNA, precursor to + H2O
?
show the reaction diagram
-
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
-
-
?
4.5S RNA, precursor to + H2O
?
show the reaction diagram
-
generation of the 5'-terminus of the mature molecule
-
-
?
C4 antisense RNA + H2O
?
show the reaction diagram
-
from bacteriophages P1 and P7
-
-
?
chloroplastic pre-tRNAPhe + H2O
chloroplastic tRNAPhe + 5' leader of tRNA
show the reaction diagram
-
-
-
-
?
deproteinized pre-rRNA + H2O
mature deproteinized rRNA + 5'-oligonucleotide
show the reaction diagram
-
large number of discrete cleavage sites
-
-
?
hepatitis C virus RNA + H2O
?
show the reaction diagram
-
the catalytic RNase P RNA cleaves near the AUG start codon
-
-
?
influenza virus mRNA + H2O
?
show the reaction diagram
-
-
-
-
?
influenza virus mRNA + H2O
?
show the reaction diagram
-
cells transfected with virus
-
-
?
pbuE adenine riboswitch + H2O
?
show the reaction diagram
Bacillus subtilis, Bacillus subtilis 1A40
-
RNase P cleaves in vitro the adenine riboswitch upstream of the pbuE gene which codes for an adenine efflux pump
-
-
?
phage antisense RNA (C4) + H2O
?
show the reaction diagram
-
-
-
-
?
phage f2RNA + H2O
?
show the reaction diagram
Escherichia coli, Escherichia coli MRE, Escherichia coli MRE600
-
degradation to a more limited extent than tRNA precursor
-
-
?
phi80-induced RNA + H2O
?
show the reaction diagram
Escherichia coli, Escherichia coli MRE, Escherichia coli MRE600
-
degradation to a more limited extent than tRNA precursor
-
-
?
polycistronic his operon mRNA precursor + H2O
?
show the reaction diagram
-
-
-
-
?
polycistronic mRNA precursor + H2O
mature mRNAs + ?
show the reaction diagram
-
RNA processing
-
-
?
pre-rRNA + H2O
mature rRNA
show the reaction diagram
-
enzyme RNase MRP plays an important role in pre-rRNA processing
-
-
?
pre-rRNA + H2O
mature rRNA
show the reaction diagram
-
RNase MRP
-
-
?
pre-rRNA + H2O
mature rRNA + 5'-oligonucleotide
show the reaction diagram
-
RNase MRP
-
-
?
pre-rRNA + H2O
?
show the reaction diagram
-
RNase MRP is involved with the maturation of pre-rRNA but cleaves RNA primers in mitochondria and localizes to cytoplasmic P-bodies where it takes part in cell cycle-regulated turnover of selected mRNAs
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
Clostridium innocuum, Mycoplasma iowae, Mycoplasma buccale
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
Q6MRS3
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
P43039
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
P75111
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
P47703
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
Q9PPN6
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
Q4A5G4
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
Q6KH14
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
Q98R57
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
Q4A750
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
Q8EU90
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
in addition to its essential role in the biosynthesis of tRNA, RNase P may have another function in vivo, namely, in the physiology of viral infections
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
removal of a 5' leader sequence from tRNA precursor
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
autoantigenic properties of the protein subunits Rpp38 and Rpp30 of catalytically active complexes of human ribonuclease P
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
involved in biosynthesis of KB cell tRNA
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
RNase P is a key enzyme acting early in the tRNA biogenesis pathway, which catalyses the endonucleolytic cleavage of the 5' leader sequence of precursor tRNAs and generates their 5' mature end
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
RNase P is responsible for the 5'-end maturation of precursor tRNAs
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
the RNase P ribozyme and the holoenzyme demonstrate strict shape specificity towards these RNAs, but the holoenzyme cannot distinguish a pre-tRNA from a hairpin RNA mimicking the top half of a pre-tRNA, both the ribozyme and the holoenzyme prefer longer acceptor-stem RNAs to shorter
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
catalyzes 5' maturation of tRNAs. RNA component of RNase P is essential for pre-tRNA cleavage
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
removes 5' extensions from genuine mitochondrial tRNA precursors
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
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 + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
the base at N-1 in the pre-tRNA interacts with A248 in the RNase P RNA
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
Saccharomyces cerevisiae YSW1
-
-
-
-
?
pre-tRNA + H2O
mature tRNA + 5'-terminal oligonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
mat-tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
?
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
?
show the reaction diagram
-
ribonucleoprotein enzyme required for 5'-end maturation of precursor tRNAs (pre-tRNAs)
-
-
?
pre-tRNA + H2O
?
show the reaction diagram
-
in mitochondria, RNase P function has been taken over by an unrelated, protein-only enzyme activity
-
-
?
pre-tRNA + H2O
tRNA
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
tRNA
show the reaction diagram
-
Ribonuclease P (RNase P) is a ribozyme that is responsible for thematuration of 5' termini of tRNA molecules
-
-
?
pre-tRNA + H2O
tRNA + RNA sequence
show the reaction diagram
-
a pre-tRNA is trapped on the CCA site and 5'-leader site first to form the Michaelis-complex. On this step, the shape of a substrate RNA is not recognized by the enzyme. After that, the T-arm site and the bottom half site cooperatively examine the shape of the substrate to achieve the transition state conformation. After the cleavage of the 5'-leader sequence, the enzyme-product complex turns to the non-transition state conformation, and the cleaved product is released from the enzyme
-
-
?
pre-tRNA + H2O
tRNA + 5' leader of tRNA
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5' leader of tRNA
show the reaction diagram
Pyrobaculum sp.
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5' leader of tRNA
show the reaction diagram
-
RNase P holoenzymes, reconstituted in vitro
-
-
?
pre-tRNA mimic + H2O
?
show the reaction diagram
-
small bipartite model substrate, smallest mimic of natural enzyme substrate consisting of a 4 bp stem and a 1 nucleotide 5'-flank, specific trans-cleavage at the canonical enzyme cleavage site
-
-
?
pre-tRNA mimic + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
mimic of natural enzyme substrate consisting of a 7 bp stem and a 3 nucleotide 5'-flank
-
-
?
pre-tRNA mimic b + H2O
?
show the reaction diagram
-
mimic of natural enzyme substrate consisting of a 7 bp stem and a 1 nucleotide 5'-flank
-
-
?
pre-tRNA mimic c + H2O
?
show the reaction diagram
-
mimic of natural enzyme substrate consisting of a 4 bp stem and a 3 nucleotide 5'-flank
-
-
?
pre-tRNA mimic d + H2O
?
show the reaction diagram
-
mimic of natural enzyme substrate consisting of a 4 bp stem and a 1 nucleotide 5'-flank
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
-
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
-
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
-
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
O59425
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
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
show the reaction diagram
-
wild-type E. coli SuIIItRNATyr precursor
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
T4-encoded dimeric tRNA precursor
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
cleaves synthetic pre-tRNAAsp by a single endonucleolytic action to generate 5'-end matured tRNA and an intact 5' leader
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
single endonucleolytic scission in E. coli tRNATyr precursor, thereby separating the 41 extra nucleotides on the 5' end of the precursor molecule from the 5' terminal sequence of the mature tRNATyr molecule
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
truncated tRNA precursor molecule that contains only aminoacyl and T stems of the tRNA moiety and the T loop with the 5' extra sequence covalently linked to nucleotide 1 of the usual mauture tRNA sequence
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
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
show the reaction diagram
-
cleaves the precursor to E. coli suppressor tRNATyr at the same site as E. coli RNase P
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
cleaves the precursor to E. coli suppressor tRNATyr at the same site as E. coli RNase P
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
Schizosaccharomyces pombe tRNA precursor derived from the sup S1 and sup3-e tRNASer genes
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
cleaves the precursor to Schizosaccharomyces pombe suppressor tRNASer at the same site as Schizosaccharomyces pombe RNase P, producing the mature 5' end of tRNASer
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
naturally occuring and selectively altered precursor tRNA molecules. Alterations in the intervening sequence reduce the susceptibility of the substrate to cleavage by RNase P
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
pre-tRNAAsp
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
bacteriophage phi80-induced RNA which is 62 nucleotides long
cleaves bacteriophage phi80-induced RNA which is 62 nucleotides long to yield two specific fragments 25 and 37 nucleotides long
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
Synechocystis 6803 precursor tRNAGln
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
the enzyme cleaves only a single phosphodiester bond of the 129 nucleotide tyrosine tRNA precursor molecule. This cleavage removes all extra nucleotides present at the 5'-terminus of the precursor as a 41 nucleotide fragment, exposing the 5'-end of the mature tRNA
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
E. coli tRNATyr precursor
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
E. coli tRNATyr precursor
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
E. coli tRNATyr precursor
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
cleaves the G residue at the +1 position in pre-tRNAHis
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
tRNAHis wild-type precursor is processed to afford a single tRNA product containing 8 base pairs in the acceptor stem. A mutant tRNAHis precursor containing a G27A alteration is processed at A27 under conditions consistent with formation of an A27-C100 base pair in the acceptor stem, but at G28 under conditions that disfavor base pair formation
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
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
show the reaction diagram
-
Gln-Leu tRNA dimeric precursor from bacteriophage T4-infected E. coli
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
substrates consisting of a short 5' ss region followed by a stem-loop structure and ending in CCA, can be cleaved by M1 RNA or the holoenzyme complex. As few as two nucleotides are required in the 5' ss region and six base pairs are needed in the stem region of the substrate
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
M1 RNA alone and the RNAse P holoenzyme from E. coli cleave the tRNA-like structure of TYMV RNA in vitro at the 5'-side of the quasi-helical structure to generate 5'-phosphate and 3'-hydroxyl groups in the cleavage products. The intact pseudoknot structure in the substrate is not required for the reaction catalyzed by M1 RNA alone, but its presence markedly improves the efficiency of the reaction
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
only slightly influenced by the T-stem sequence, but critically dependent on the presence of the 3'-terminal CCA end
-
-
-
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
pTyrA54, a mutant tRNA precursor with a base change that can potentially complement the U334 mutation in M1 RNA
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
the enzyme cleaves precursor RNA terminating in either CCA or UAA to generate the 5'-termini characteristic of both mature RNA species: Kinetically favors precursor RNA ending CCA over that ending UAA
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
pre-tRNATyr
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
pre-tRNATyr
-
-
ir
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
pre-tRNATyr
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
pre-tRNATyr
-
-
-
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
E. coli tRNATyr
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
RNAs in a T-shape structure can be substrates for the ribozyme reactions even at low concentrations of magnesium ions. The RNA in a natural L-shape is the best substrate for both the ribozyme and the holo enzyme
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
Q8U0H6
cleaves the 5'-leader sequence of precursor tRNAs during their maturation
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
Escherichia coli MRE
-
the enzyme cleaves only a single phosphodiester bond of the 129 nucleotide tyrosine tRNA precursor molecule. This cleavage removes all extra nucleotides present at the 5'-terminus of the precursor as a 41 nucleotide fragment, exposing the 5'-end of the mature tRNA, pre-tRNATyr
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
Escherichia coli MRE600
-
the enzyme cleaves precursor RNA terminating in either CCA or UAA to generate the 5'-termini characteristic of both mature RNA species: Kinetically favors precursor RNA ending CCA over that ending UAA
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
Escherichia coli MRE600
-
the enzyme cleaves only a single phosphodiester bond of the 129 nucleotide tyrosine tRNA precursor molecule. This cleavage removes all extra nucleotides present at the 5'-terminus of the precursor as a 41 nucleotide fragment, exposing the 5'-end of the mature tRNA, pre-tRNATyr
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
Bacillus subtilis 1A40
-
-
-
-
?
pre-tRNA precursor + H2O
mat-tRNA + RNA
show the reaction diagram
-
-
-
-
?
pre-tRNA-Gly + H2O
tRNA-Gly + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA-Gly + H2O
tRNA-Gly + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA-Met + H2O
tRNA-Met + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA-Tyr + H2O
tRNA-Tyr + 5'-oligoribonucleotide
show the reaction diagram
Saccharomyces cerevisiae, Saccharomyces cerevisiae SCWY10
-
-
-
-
?
pre-tRNA-Val + H2O
tRNA-Val + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA3Pro + H2O
mature tRNA3Pro + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNAAla + H2O
mature tRNAAla + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide of fly substrate, hyperprocessing
generates 5'-phosphate,3'-hydroxyl-product
-
?
pre-tRNAAsp + H2O
tRNAAsp + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
-
pre-tRNAAsp + H2O
tRNAAsp + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNAAsp + H2O
tRNAAsp + 5'-oligoribonucleotide
show the reaction diagram
-
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
show the reaction diagram
-
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. Sequence preference of RNase P shows a weak preference for adenosine and cytosine at N(-4). Higher binding affinity for A(-4) and C(-4) pre-tRNAs relative to that for G(-4) and U(-4), with an overall preference of 5fold. L34 contributes to selectivity
-
-
?
pre-tRNAAsp + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
5' fluorescein-labeled Bacillus subtilis pre-tRNAAsp (Fl-pre-tRNA) possessing a 5-nucleotide leader
-
-
?
pre-tRNAAsp + H2O
tRNAsp + 5'-oligoribonucleotide
show the reaction diagram
-
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
-
-
?
pre-tRNAHis + H2O
mature tRNAHis + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide of fly substrate, hyperprocessing
generates 5'-phosphate,3'-hydroxyl-product
-
?
pre-tRNALeu + H2O
tRNALeu + 5' leader of tRNA
show the reaction diagram
Ostreococcus tauri, Ostreococcus tauri RCC745
Q00XA5
-
-
-
?
pre-tRNAMet_ini + H2O
mature tRNAMet_ini + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide of fly initiator methionine tRNA, hyperprocessing
generates 5'-phosphate,3'-hydroxyl-product
-
?
pre-tRNAPhe + H2O
?
show the reaction diagram
Q9X1H4
-
-
-
?
pre-tRNAPhe + H2O
tRNAPhe + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNATyr + H2O
mature tRNATyr + 5'-oligoribonucleotide
show the reaction diagram
O59543
substrate from Pyrococcus horikoshii OT3, cleavage of 5'-terminal oligonucleotide
generates 5'-phosphate,3'-hydroxyl-product
-
?
pre-tRNATyr + H2O
mature tRNATyr + 5'-oligoribonucleotide
show the reaction diagram
-
cleaves efficiently at a single phosphodieste bond between positions U59 and C60
-
-
?
pre-tRNATyr + H2O
mature tRNATyr + 5'-oligoribonucleotide
show the reaction diagram
-
is completely processed. Cleaves efficiently at a single phosphodieste bond between positions U59 and C60
-
-
?
pre-tRNATyr + H2O
mature tRNATyr + 5'-oligoribonucleotide
show the reaction diagram
-
two chimeric RNAs, in which the functional C- and S-domains of Escherichia coli RNase P RNA and Pyrococcus horiskoshii RNA are mutally exchanged with respect to cleavage of Pyrococcus horiskoshii pre-tRNATyr in the presence of Escherichia coli C5 protein or Pop5, Rpp21, Rpp29 and Rpp30 of Pyrococcus horiskoshii. Pop 5 and Rpp 30 function equivalently to the C5 protein, being involved in activation of the C-domain, while Rpp21 and Rpp29 are implicated in the stabilization of the RNA S-domain
-
-
?
pre-tRNATyr + H2O
mature tRNATyr + 5'-oligoribonucleotide
show the reaction diagram
-
two chimeric RNAs, in which the functional C- and S-domains of Escherichia coli RNase P RNA and Pyrococcus horiskoshii RNA are mutally exchanged with respect to cleavage of Pyrococcus horiskoshii pre-tRNATyr in the presence of Escherichia coli C5 protein or Pop5, Rpp21, Rpp29 and Rpp30 of Pyrococcus horiskoshii. Pop 5 and Rpp 30 function equivalently to the C5 protein, being involved in activation of the C-domain, while Rpp21 and Rpp29 are implicated in the stabilization of the RNA S-domain. RNA S-domain is more drastically unfolded by Rpp21 and Rpp29 than the RNA C-domain by Pop5 and Rpp30
-
-
?
pre-tRNATyr + H2O
mature tRNATyr + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide of human substrate, hyperprocessing
generates 5'-phosphate,3'-hydroxyl-product
-
?
pre-tRNATyr + H2O
tRNATyr + 5' leader of tRNA
show the reaction diagram
-
-
-
-
?
pre-tRNATyr + H2O
tRNATyr + 5' leader of tRNA
show the reaction diagram
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
-
activity assay using in vitro reconstituted particles
-
-
?
pre-tRNATyr + H2O
tRNATyr + 5'-oligoribonucleotide
show the reaction diagram
P62426 and P60780 and P60781 and P60832 and P62378
-
-
-
?
pre-tRNATyr + H2O
tRNATyr + 5'-oligoribonucleotide
show the reaction diagram
-
pre-tRNATyr from Escherichia coli
-
-
?
pre-tRNATyr + H2O
tRNATyr + 5'-oligoribonucleotide
show the reaction diagram
-
pre-tRNATyr from Escherichia coli
-
-
?
pre-tRNATyr + H2O
tRNATyr + 5'-oligoribonucleotide
show the reaction diagram
-
pre-tRNATyr from Escherichia coli
-
-
?
pre-tRNATyr precursor + H2O
mature tRNATyr + 5'-terminal oligonucleotide
show the reaction diagram
-
-
-
-
?
precursor tRNA + H2O
77- and 35-RNA fragments
show the reaction diagram
-
ribonuclease P is the endonuclease that removes the leader fragments from the 5'-ends of precursor tRNAs
-
-
?
precursor tRNA + H2O
?
show the reaction diagram
-
catalyze the 5' maturation of precursor tRNA
-
-
?
precursor tRNA + H2O
?
show the reaction diagram
-
catalyzes the magnesium-dependent 5'-end maturation of tRNAs
-
-
?
precursor tRNA + H2O
?
show the reaction diagram
-
RNase P is an endoribonuclease responsible for generating the 5' end of mature tRNA molecules and, in bacteria, this ribonucleoprotein complex consists of a basic protein and an RNA moiety in a 1:1 ratio
-
-
?
precursor tRNA + H2O
?
show the reaction diagram
-
cleavage of precursor tRNAs with an LNA (extra methylene), 2'-OCH3, 2'-H or 2'-F modification at the canonical (c0) site by type A RNase P RNA. Extent of cleavage for the LNA (T-1) and 2'-OCH3 (T-1) substrates is extremely low. LNA and 2'-OCH3 suppress processing at the major aberrant m-1 site. Instead, the m+1 (nt +1/+2) site is utilized
-
-
?
precursor tRNA + H2O
?
show the reaction diagram
-
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
-
-
?
precursor tRNA + H2O
?
show the reaction diagram
-
RNase P holoenzyme (M1 RNA and C5 protein) primarily recognizes the acceptor stem and possibly the T-stem loop regions in precursor tRNAs. Both M1 RNA and C5 are essential for RNase P activity. Interaction between the 3' RCCA sequence and RNase P is essential for cleavage of tRNA precursors. Does not cleave the internal ribosome entry site region in hepatitis C virus RNA. Linkage of the catalytic M1 RNA and the external guide sequence, making an M1 guide sequence (GS) construct, which ensures close contact of the catalytic M1 RNA with the target cleavage site when the guide sequence is hybridized to its target RNA
-
-
?
precursor tRNA Gly + H2O
mature tRNA Gly + 5'-GGAUUUUCCCUUUC
show the reaction diagram
-
-
5' flank with homogeneous 3' end, CCAGUC-3'
-
?
precursors to 4.5 S RNA + H2O
?
show the reaction diagram
-
-
-
-
?
ptRNATyr + H2O
?
show the reaction diagram
-
from Escherichia coli, from Eschericha coli
-
-
?
ssRNA oligonucleotide + H2O
5'-phospho-3'-hydroxy-ribonucleotides
show the reaction diagram
-
holoenzyme, specificity with different ssRNA substrates, determination of cleavage sites, overview
-
-
?
SupS1 precursor + H2O
?
show the reaction diagram
-
-
-
-
?
syntaxin18 mRNA + H2O
?
show the reaction diagram
-
-
-
-
?
tmRNA + H2O
?
show the reaction diagram
-
-
-
-
?
tmRNA precursor + H2O
mature tmRNA + 5'-oligonucleotide
show the reaction diagram
-
RNA processing
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
5'-leader sequence tRNA processing, essential enzyme
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide, maturation
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide, maturation
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide, maturation
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide, maturation
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide, maturation, essential
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide, maturation, essential
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide, maturation, essential
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
essential enzymes in the biogenesis of tRNA, maturation
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
tRNA processing
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
tRNA processing
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
tRNA processing
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
tRNA processing
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
O59543
tRNA processing
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
tRNA processing, the premature substrate is associated with a complex of 7 Sm-like proteins, i.e. Lsm2-8, and U6 snRNA
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide, cleavage site
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide, reconstituted mini-enzyme and wild-type enzyme, both cleave at positions G28-G29
generates 5'-phosphate,3'-hydroxyl-product, reconstituted mini-enzyme and wild-type enzyme
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide, the 5'leader of the pre-tRNA substrate is recognized by the active site of the enzyme via interaction of N(-1) substrate nucleotide with A248 of the ribozyme, preference for U at position N(-1)
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
site-specific cleavage of 5'-terminal oligonucleotide from pre-tRNA, 3 potential RNA binding motifs
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNA precursor + H2O
mature tRNA + 5'-terminal oligonucleotide
show the reaction diagram
-
enzyme is responsible for removing the 5'-leader segment of precursor tRNA
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-terminal oligonucleotide
show the reaction diagram
-
enzyme is responsible for removing the 5'-leader segment of precursor tRNA during maturation
-
-
?
tRNA-like pseudoknotted structures in viral RNA + H2O
processed RNA + ?
show the reaction diagram
-
tRNA-like pseudoknotted structures in viral RNA
-
-
?
tRNAAsp precursor + H2O
mature tRNAAsp + 5'-terminal oligonucleotide
show the reaction diagram
-
sequence
5'-terminal oligonucleotide with 3'-hydroxyl and 5'-phosphoryl
-
ir
tRNAAsp precursor + H2O
mature tRNAAsp + 5'-terminal oligonucleotide
show the reaction diagram
-
sequence, potential catalytic transition state structure including 3 required divalent metal ions
5'-terminal oligonucleotide with 3'-hydroxyl and 5'-phosphoryl
-
ir
tRNALeu5 + H2O
?
show the reaction diagram
Escherichia coli, Escherichia coli MG1693
-
RNase P, the endonuclease responsible for generating mature 5' termini, also plays a role in the 3'-end processing of leuX. It removes the terminator from ca. 10% of primary transcripts by cleaving 4-7 nt downstream of the CCA determinant, generating substrates for RNase II, which removes an additional 3-4 nt
-
-
?
tRNAPhe (A+1) precursor + H2O
mature tRNAPhe + 5'-terminal oligonucleotide
show the reaction diagram
-
yeast tRNA substrate from in vitro transcription, structure
5'-terminal oligonucleotide with 3'-hydroxyl and 5'-phosphoryl, product and cleavage site determination
-
?
tRNAPhe (A+1) precursor + H2O
mature tRNAPhe + 5'-terminal oligonucleotide
show the reaction diagram
-
yeast tRNA substrate from in vitro transcription, structure, cleavage of substrate containing a pro-Rp nonbridging oxygen or, by substitution with phosphothionate, a sulfur at the scissile bond
5'-terminal oligonucleotide with 3'-hydroxyl and 5'-phosphoryl, product and cleavage site determination
-
?
tRNAPhe (G+1) precursor + H2O
mature tRNAPhe + 5'-terminal oligonucleotide
show the reaction diagram
-
yeast tRNA substrate from in vitro transcription, structure
5'-terminal oligonucleotide with 3'-hydroxyl and 5'-phosphoryl, product and cleavage site determination
-
?
tRNAPhe (G+1) precursor + H2O
mature tRNAPhe + 5'-terminal oligonucleotide
show the reaction diagram
-
yeast tRNA substrate from in vitro transcription, structure, cleavage of substrate containing a pro-Rp nonbridging oxygen or, by substitution with phosphothionate, a sulfur at the scissile bond
5'-terminal oligonucleotide with 3'-hydroxyl and 5'-phosphoryl, product and cleavage site determination
-
?
tRNAPhe precursor + H2O
mature tRNAPhe + 5'-terminal oligonucleotide
show the reaction diagram
-
maize tRNA substrate, structure
cleavage site determination
-
?
tRNATyr precursor + H2O
mature tRNATyr + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNATyr precursor + H2O
mature tRNATyr + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide, reconstituted mini-enzyme and wild-type enzyme, both cleave at positions G28-G29
generates 5'-phosphate,3'-hydroxyl-product, reconstituted mini-enzyme and wild-type enzyme
-
?
tRNATyr precursor + H2O
mature tRNATyr + 5'-oligonucleotide
show the reaction diagram
-
human substrate, cleavage of 5'-terminal oligonucleotide, enzyme recognizes the RNA substrate hairpin structure
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNATyr precursor + H2O
mature tRNATyr + 5'-terminal oligonucleotide
show the reaction diagram
-
-
-
-
?
tRNATyrUAG precursor + H2O
?
show the reaction diagram
-
RNase P cleavage of this substrate generates a 5' matured tRNA with a 7 base pair amino acceptor stem
-
-
?
mitochondrial pre-tRNACys + H2O
mitochondrial tRNACys + 5' leader of tRNA
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
structures of the acceptor stem and anticodon/intron loop of the tRNA are crucial for Schizosaccharomyces pombe RNase P action
-
-
-
additional information
?
-
-
biosynthesis and regulation of RNase P, transient interactions with several proteins in the cell, the protein subunits are conserved between RNase P and RNase MRP, and are essential for cell viability and enzyme function, overview, enzyme subunits in nucleolus and Cajal bodies might be involved in cell mitosis and cell-cycle-dependent gene transcription
-
-
-
additional information
?
-
-
coordination of RNA pathways, overview
-
-
-
additional information
?
-
-
other pre-RNAs are also physiological substrates of the enzyme
-
-
-
additional information
?
-
-
phylogenetic study of archeal enzymes
-
-
-
additional information
?
-
-
regulation of gene expression can be achieved by creating a complex made of target mRNA and a complementary small oligonucleotide that resembels natural enzyme substrate
-
-
-
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
?
-
-
the mitochondrial ribozyme RNA subunit might have a cellular function outside the mitochondria
-
-
-
additional information
?
-
-
transient interactions with several proteins in the cell, e.g. protein subunit Rpp20 interacts with the heat shock protein Hsp27, protein subunit Rpp14 interacts with several proteins including the LIM domain protein 1 LIMD1 and the SR-rich HSPC232
-
-
-
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
?
-
-
external guide sequences EGS can bind to complementary sequence of substrate ssRNA and thereby target the enzyme to specific cleavage sites
-
-
-
additional information
?
-
-
hyperprocessing occurs with tRNA molecules denatured to form double-hair pin-like structures, instead of cloverleaf structure, reaction mechanism
-
-
-
additional information
?
-
-
no activity with substrates in which the pro-Rp or pro-Sp nonbridging oxygen of the scissile bond is replaced by sulfur, substitution via phosphothionate
-
-
-
additional information
?
-
-
protein subunit Rpp20 also acts as an ATPase, protein subunits Rpp14, Rpp21, and Rpp29 are responsible for pre-tRNA substrate binding
-
-
-
additional information
?
-
-
protein subunits Rpp21 and Rpp29 and RNA subunit H1 are sufficient for effective substrate cleavage, thereby the protein subunits facilitate catalytic activity of RNA subunit H1 which requires a phylogenetically conserved pseudoknot-structure for function, protein subunit Rpp29 formsa catalytic complex with M1 RNA from Escherichia coli
-
-
-
additional information
?
-
-
recognition of bipartite substrates and chimera constructed from external guide sequences EGS and ssRNA
-
-
-
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
?
-
-
substrate specificities of enzyme forms RNase P and RNase MRP
-
-
-
additional information
?
-
-
targeting of any mRNA for cleavage by the enzyme with aid of external guide sequences EGS, e.g. EGS with chloramphenicol acetyltransferase mRNA from cat, or EGS with gyrase A mRNA from Salmonella typhimurium, forming a complex with the complementary RNA substrate sequence, overview
-
-
-
additional information
?
-
-
the recombinant holoenzyme and the Rpp20p subunit display ATPase activity
-
-
-
additional information
?
-
-
the RNA subunit alone is not active
-
-
-
additional information
?
-
-
the RNA subunit can cleave tRNA substrate in absence of the protein subunit
-
-
-
additional information
?
-
-
the RNA subunit is the catalytic subunit, while the protein subunits are essential for substrate binding, broad substrate specificity
-
-
-
additional information
?
-
-
catalytic RNase P RNA does not cleave hepatitis C virus RNA
-
-
-
additional information
?
-
-
RNase P cleaves transient structures in some riboswitches
-
-
-
additional information
?
-
-
5'-maturation of transfer RNA
-
-
-
additional information
?
-
-
5-maturation of transfer RNA
-
-
-
additional information
?
-
-
catalyses the 5'-end processing reaction of tRNA precursor molecules
-
-
-
additional information
?
-
-
catalyze tRNA 5-end maturation
-
-
-
additional information
?
-
-
catalyzes the 5-end maturation of tRNAs in all Kingdoms of life
-
-
-
additional information
?
-
-
essential ribonucleoprotein enzyme responsible for the 5'-end maturation of tRNAs
-
-
-
additional information
?
-
-
involved in regulation of noncoding RNA (ncRNA) expression
-
-
-
additional information
?
-
-
expression validated by Northern blotting, transcription initiation sites mapped by primer extension and RNase protection assay, secondary structure deduced, longer and more complex P3 helix-loop-helix structures compared to vertebrates
-
-
-
additional information
?
-
-
the human mitochondrial RNase P is an entirely protein-based enzyme, protein MRPP1, a probable tRNA methylase, provides tRNA-binding specificity to the RNase P enzyme, protein MRPP2 binds tightly to MRPP1 and is a member of the short chain dehydrogenase/reductase protein family, protein MRPP3 may provide the enzymatic cleavage activity for the patchwork enzyme
-
-
-
additional information
?
-
-
M1GS RNA cleaves the overlapping mRNA region of two murine cytomegalovirus capsid proteins essential for viral replication: the assembly protein (mAP) and M80
-
-
-
additional information
?
-
-
RNase P cleaves the mRNAs of Yersinia pestis yscN and yscS genes in vitro with the cognate external guide sequences resulting in the reduction of the levels of these messages of the virulence genes when those genes are expressed in Escherichia coli
-
-
-
additional information
?
-
-
RNase P RNA is a substrate of the DEAD box helicase Hera, the specificity of Hera for RNase P RNA may be required for RNase P RNA folding or RNase P assembly
-
-
-
additional information
?
-
-
the guanine riboswitch encoded upstream of xpt-pbuX operon, is not cleaved
-
-
-
additional information
?
-
-
cleavage of target RNA by RNase P is induced when three-fourths of a tRNA is used as an external guide sequence. RNase P enzyme seems to have lost the RNA component during evolution, proving that the catalytic activity of the RNA component of the RNase P holoenzyme can be accomplished by proteins alone. RNase P is able to cleave a model substrate containing only the acceptor stem, a 1 nucleotide (A or C) bulge and the T stem-loop. Cleavage of target RNAs is enhanced if the external guide sequence also contains a variable loop and form a D-like stem with the target, as a minimized 3/4 external guide sequence. Cleaves the internal ribosome entry site region in hepatitis C virus RNA. RNase P-mediated inhibition of mRNAs involved in cancer
-
-
-
additional information
?
-
-
cleaves riboswitchs
-
-
-
additional information
?
-
-
cleaves the internal ribosome entry site region in hepatitis C virus RNA near the AUG start codon
-
-
-
additional information
?
-
synthetic construct
-
in vitro cleavage of human cytomegalovirus mRNA sequence by M1GS ribozyme. Incubation of a substrate containing the capsid scaffolding protein mRNA sequence with functional ribozyme M1-C1 (3'-terminus of an engineered M1GS ribozyme, V57, covalently linked with a guide sequence of 18 nucleotides that is complementary to the targeted mRNA sequence) yields efficient cleavage. Cleavage of capsid scaffolding protein mRNA by mutant M1-C2 or M1-thymidine kinase is barely detected
-
-
-
additional information
?
-
-
interaction of four RNase P proteins (Pop5, Rpp21, Rpp29 and Rpp30) with RNase P RNA results in destabilization of base stacking in RNase P RNA, wheras addition of a fifth protein (Rpp38) increases base stacking of RNase P RNA
-
-
-
additional information
?
-
-
interaction of immobilized RNase P protein and 3'-biotinylated RNase P RNA bound to streptavidin-coated magnetic beads. The protein binds to the C-domain of P RNA in the P2-J2/3-P3-J3/4-P4-J18/2 region. Kd values of about 1-2 nanomol (at 4.5 mM Mg2+ and 150 mM NH4+) for RNase P RNA and protein. A bacterial-like 1-bp insertion and 2-nt deletion in the helix P2/P3 region largely improves affinity, thus these elements are crucial for interaction of the two RNase P subunits
-
-
-
additional information
?
-
-
is unable to activate non-cognate RNase P RNAs, Pyrococcus horikoshii RNase P RNA and Escherichia coli RNase P RNA. Chimeric RNase P RNAs composed of the Escherichia coli RNA C-domain and Pyrococcus horikoshii S-domain or composed of the Pyrococcus horikoshii C-domain and Escherichia coli RNA S-domain, respectively, exhibit activity. C5 protein is involved in activation of the Escherichia coli pRNA C-domain
-
-
-
additional information
?
-
-
M1GSs directed against BCR-ABL chimeric RNAs are efficient in specifically cleaving the chimeric RNA transcripts. M1GS directed against the thymidine kinase mRNA from herpes simplex virus 1 is able to reduce the thymidine kinase mRNA and protein level with 80%. Efficiency of inhibition can be improved to above 90% reduction in mRNA and protein level, and 4000fold reduction in herpes simplex virus 1 viral load, using an M1GS ribozyme optimized through in vitro selection
-
-
-
additional information
?
-
-
RNase P enzyme seems to have lost the RNA component during evolution, proving that the catalytic activity of the RNA component of the RNase P holoenzyme can be accomplished by proteins alone
-
-
-
additional information
?
-
-
RNase P proteins Pop5, Rpp21, Rpp29, Rpp30 and Rpp38 are unable to activate non-cognate RNase P RNAs, Pyrococcus horikoshii RNase P RNA and Escherichia coli RNase P RNA. Chimeric RNase P RNAs composed of the Escherichia coli RNA C-domain and Pyrococcus horikoshii S-domain or composed of the Pyrococcus horikoshii C-domain and Escherichia coli RNA S-domain, respectively, exhibit activity. Pop5 and Rpp30 are involved in activation of the Pyrococcus horikoshii pRNA C-domain, whereas Rpp21 and Rpp29 are implicated in stabilization of the Pyrococcus horikoshii pRNA S-domain
-
-
-
additional information
?
-
-
Rpp20 and Rpp25 interact with the P3 arm of RNase MRP RNA in a highly synergic fashion. Rpp20 and Rpp25 interact with the P3 RNA as a heterodimer, which is formed prior to RNA binding
-
-
-
additional information
?
-
-
yeast RNase P may process antisense RNAs from genes encoding ribosomal proteins
-
-
-
additional information
?
-
-
an external guide sequence, EGS, RNA base-paired to a target RNA makes the latter a substrate for endogenous RNase P by rendering the bipartite target RNA-EGS complex a precursor tRNA structural mimic. RNase P holoenzymes recognize and cleave such substrate-EGS complexes. The external guide sequences engage in multiple rounds of substrate recognition while assisting archaeal RNase P-mediated cleavage of a target RNA in vitro
-
-
-
additional information
?
-
-
only a small fraction of the mixed-sequence RNA is cleaved by RNase P. Binding and cleavage of unstructured RNA by nuclear RNase P, overview
-
-
-
additional information
?
-
-
5'-endonucleolytic precursor tRNA cleavage
-
-
-
additional information
?
-
-
precursor tRNAs are natural enzyme RNase P substrates
-
-
-
additional information
?
-
-
ribonuclease P catalyzes the metal-dependent 5' end maturation of precursor tRNAs
-
-
-
additional information
?
-
-
RNase P is the endonuclease that removes 5' extensions from tRNA precursors
-
-
-
additional information
?
-
-
the enzyme catalyzes the 5' end maturation of precursor tRNAs (pre-tRNAs)
-
-
-
additional information
?
-
-
the enzyme is a ribonuleoprotein that catalyzes the processing of 5' leader sequences from tRNA precursors and other noncoding RNA
-
-
-
additional information
?
-
Q9X1H4
the enzyme is an RNA-based enzyme primarily catalyzing 5'-end pre-tRNA processing
-
-
-
additional information
?
-
-
the enzyme processes the 5' ends of tRNA precursors, the substrate population includes over 80 different competing ptRNAs in Escherichia coli, sequence and secondary structure of representative ptRNAs, overview. Its mode of molecular recognition differs from other catalytic RNAs in two important ways. First, its biological role in ptRNA processing requires that it act in trans as a multiple turnover enzyme, whereas other ribozymes, with the exceptions of the ribosome and spliceosome, undergo single turnover self-splicing or self-cleavage reactions. Second, RNase P processes multiple RNA substrates, including all ptRNAs in the cell, whereas other ribozymes, again with the exceptions of the ribosome and spliceosome, have one specific substrate
-
-
-
additional information
?
-
-
the enzyme processes the 5'-end of tRNAs
-
-
-
additional information
?
-
L0N807
the enzyme processes the 5'-end of tRNAs
-
-
-
additional information
?
-
-
the mechanism by which the enzyme processes the valU and lysT polycistronic transcripts (valV valW, valU valX, valY lysY and lysT valT lysW valZ lysY lysZ lysQ) involves initiation of processing by first endonucleolytically removing the Rho-independent transcription terminators from the primary valU and lysT transcripts. Subsequently, the enzyme proceeds in the 3' -> 5' direction generating one pre-tRNA at a time. Identification of cleavage sites using RNA circularization, overview
-
-
-
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
-
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
-
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
-
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
-
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
-
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
-
additional information
?
-
-
the natural substrate is precursor tRNA. Proteinaceous PRORP1 catalyzes all of the other noncanonical, yet vital functions of nuclear yeast RNase P, which may include processing of non-canonical RNAs
-
-
-
additional information
?
-
-
assay substrate is tobacco chloroplast precursor tRNAGly
-
-
-
additional information
?
-
-
constructed substrate: a hybridized complex of an external guide sequence and a target RNA, e.g. mRNA, that resembles the structure of a tRNA, structure overview
-
-
-
additional information
?
-
-
construction of a modell substrate for M1 RNA from Escherichia coli. wild-type and mutant enzymes cleave the HIV RNA sequence in the tat region. The variant, containing combined mutations at nucleotide 83 and 340 of RNase P catalytic RNA, cleaves the tat RNA sequence in vitro about 20 times more efficiently than the wild-type ribozyme
-
-
-
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
?
-
-
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 under multiple-turnover conditions
-
-
-
additional information
?
-
-
method development for the engineered catalytic RNA subunit of Escherichia coli RNase P to cleave tRNA-like substrates and other target RNAs, including specific mRNAs, detailed overview
-
-
-
additional information
?
-
-
substrate is a RNA-tRNA primary transcript
-
-
-
additional information
?
-
-
substrate used in assays is Escherichia coli pre-tRNATyr
-
-
-
additional information
?
-
Q66GI4
substrates are mitochondrial tRNACys precursor variants
-
-
-
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
-
-
-
additional information
?
-
-
the enzyme PRORP1 cleaves pre-tRNAs substrates lacking an anticodon arm, the recognition mechanism involves the D-TpsiC loops in tRNA, overview. It is also active on Thermus thermophilus pre-tRNAGly
-
-
-
additional information
?
-
-
the enzyme PRORP1 cleaves pre-tRNAs substrates lacking an anticodon arm,n recognition mechanism involves the D-TpsiC loops in tRNA, overview
-
-
-
additional information
?
-
-
the ptRNA substrates are 5'-end-labeled with [gamma-32P]ATP and T4 polynucleotide kinase, after dephosphorylation by alkaline phosphatase, in reaction with RNase P holoenzyme
formation of products from two substrates independently in the same reaction, ptRNAfMet47 and ptRNAMet82 are modified for eparation by PAGE by the addition of two extra G nucleotides to the 5' end of the leader sequence, giving rise to ptRNAfMet47(+2) and ptRNAMet82(+2)
-
-
additional information
?
-
-
usage of model hairpin loop RNA substrates, e.g. pMini3bpUG, pATSerCG or pATSerUG, secondary structures, overview
-
-
-
additional information
?
-
Escherichia coli MG1693
-
the mechanism by which the enzyme processes the valU and lysT polycistronic transcripts (valV valW, valU valX, valY lysY and lysT valT lysW valZ lysY lysZ lysQ) involves initiation of processing by first endonucleolytically removing the Rho-independent transcription terminators from the primary valU and lysT transcripts. Subsequently, the enzyme proceeds in the 3' -> 5' direction generating one pre-tRNA at a time. Identification of cleavage sites using RNA circularization, overview
-
-
-
additional information
?
-
Bacillus subtilis 1A40
-
the guanine riboswitch encoded upstream of xpt-pbuX operon, is not cleaved
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
10Sa RNA + H2O
?
show the reaction diagram
-
-
-
-
?
4.55 rRNA precursor + H2O
mature 4.55 rRNA + 5'-oligonucleotide
show the reaction diagram
-
-
-
-
?
4.5S RNA precursor + H2O
mature 4.5S RNA + 5'-oligonucleotide
show the reaction diagram
-
RNA processing
-
-
?
polycistronic his operon mRNA precursor + H2O
?
show the reaction diagram
-
-
-
-
?
polycistronic mRNA precursor + H2O
mature mRNAs + ?
show the reaction diagram
-
RNA processing
-
-
?
pre-rRNA + H2O
mature rRNA
show the reaction diagram
-
enzyme RNase MRP plays an important role in pre-rRNA processing
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
in addition to its essential role in the biosynthesis of tRNA, RNase P may have another function in vivo, namely, in the physiology of viral infections
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
removal of a 5' leader sequence from tRNA precursor
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
autoantigenic properties of the protein subunits Rpp38 and Rpp30 of catalytically active complexes of human ribonuclease P
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
involved in biosynthesis of KB cell tRNA
-
-
?
pre-tRNA + H2O
mature tRNA + 5'-terminal oligonucleotide
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
?
show the reaction diagram
-
ribonucleoprotein enzyme required for 5'-end maturation of precursor tRNAs (pre-tRNAs)
-
-
?
pre-tRNA + H2O
tRNA
show the reaction diagram
-
-
-
-
?
pre-tRNA + H2O
tRNA
show the reaction diagram
-
Ribonuclease P (RNase P) is a ribozyme that is responsible for thematuration of 5' termini of tRNA molecules
-
-
?
precursor tRNA + H2O
77- and 35-RNA fragments
show the reaction diagram
-
ribonuclease P is the endonuclease that removes the leader fragments from the 5'-ends of precursor tRNAs
-
-
?
precursor tRNA + H2O
?
show the reaction diagram
-
catalyze the 5' maturation of precursor tRNA
-
-
?
precursor tRNA + H2O
?
show the reaction diagram
-
catalyzes the magnesium-dependent 5'-end maturation of tRNAs
-
-
?
precursor tRNA + H2O
?
show the reaction diagram
-
RNase P is an endoribonuclease responsible for generating the 5' end of mature tRNA molecules and, in bacteria, this ribonucleoprotein complex consists of a basic protein and an RNA moiety in a 1:1 ratio
-
-
?
ptRNATyr + H2O
?
show the reaction diagram
-
from Escherichia coli, from Eschericha coli
-
-
?
tmRNA precursor + H2O
mature tmRNA + 5'-oligonucleotide
show the reaction diagram
-
RNA processing
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
5'-leader sequence tRNA processing, essential enzyme
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide, maturation
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide, maturation
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide, maturation
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide, maturation
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide, maturation, essential
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide, maturation, essential
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
cleavage of 5'-terminal oligonucleotide, maturation, essential
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
essential enzymes in the biogenesis of tRNA, maturation
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
tRNA processing
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
tRNA processing
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
tRNA processing
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
tRNA processing
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
O59543
tRNA processing
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
show the reaction diagram
-
tRNA processing, the premature substrate is associated with a complex of 7 Sm-like proteins, i.e. Lsm2-8, and U6 snRNA
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-terminal oligonucleotide
show the reaction diagram
-
enzyme is responsible for removing the 5'-leader segment of precursor tRNA
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-terminal oligonucleotide
show the reaction diagram
-
enzyme is responsible for removing the 5'-leader segment of precursor tRNA during maturation
-
-
?
tRNA-like pseudoknotted structures in viral RNA + H2O
processed RNA + ?
show the reaction diagram
-
tRNA-like pseudoknotted structures in viral RNA
-
-
?
C4 antisense RNA + H2O
?
show the reaction diagram
-
from bacteriophages P1 and P7
-
-
?
additional information
?
-
-
biosynthesis and regulation of RNase P, transient interactions with several proteins in the cell, the protein subunits are conserved between RNase P and RNase MRP, and are essential for cell viability and enzyme function, overview, enzyme subunits in nucleolus and Cajal bodies might be involved in cell mitosis and cell-cycle-dependent gene transcription
-
-
-
additional information
?
-
-
coordination of RNA pathways, overview
-
-
-
additional information
?
-
-
other pre-RNAs are also physiological substrates of the enzyme
-
-
-
additional information
?
-
-
phylogenetic study of archeal enzymes
-
-
-
additional information
?
-
-
regulation of gene expression can be achieved by creating a complex made of target mRNA and a complementary small oligonucleotide that resembels natural enzyme substrate
-
-
-
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
?
-
-
the mitochondrial ribozyme RNA subunit might have a cellular function outside the mitochondria
-
-
-
additional information
?
-
-
transient interactions with several proteins in the cell, e.g. protein subunit Rpp20 interacts with the heat shock protein Hsp27, protein subunit Rpp14 interacts with several proteins including the LIM domain protein 1 LIMD1 and the SR-rich HSPC232
-
-
-
additional information
?
-
-
5'-maturation of transfer RNA
-
-
-
additional information
?
-
-
5-maturation of transfer RNA
-
-
-
additional information
?
-
-
catalyses the 5'-end processing reaction of tRNA precursor molecules
-
-
-
additional information
?
-
-
catalyze tRNA 5-end maturation
-
-
-
additional information
?
-
-
catalyzes the 5-end maturation of tRNAs in all Kingdoms of life
-
-
-
additional information
?
-
-
essential ribonucleoprotein enzyme responsible for the 5'-end maturation of tRNAs
-
-
-
additional information
?
-
-
involved in regulation of noncoding RNA (ncRNA) expression
-
-
-
additional information
?
-
-
the human mitochondrial RNase P is an entirely protein-based enzyme, protein MRPP1, a probable tRNA methylase, provides tRNA-binding specificity to the RNase P enzyme, protein MRPP2 binds tightly to MRPP1 and is a member of the short chain dehydrogenase/reductase protein family, protein MRPP3 may provide the enzymatic cleavage activity for the patchwork enzyme
-
-
-
additional information
?
-
-
5'-endonucleolytic precursor tRNA cleavage
-
-
-
additional information
?
-
-
precursor tRNAs are natural enzyme RNase P substrates
-
-
-
additional information
?
-
-
ribonuclease P catalyzes the metal-dependent 5' end maturation of precursor tRNAs
-
-
-
additional information
?
-
-
RNase P is the endonuclease that removes 5' extensions from tRNA precursors
-
-
-
additional information
?
-
-
the enzyme catalyzes the 5' end maturation of precursor tRNAs (pre-tRNAs)
-
-
-
additional information
?
-
-
the enzyme is a ribonuleoprotein that catalyzes the processing of 5' leader sequences from tRNA precursors and other noncoding RNA
-
-
-
additional information
?
-
Q9X1H4
the enzyme is an RNA-based enzyme primarily catalyzing 5'-end pre-tRNA processing
-
-
-
additional information
?
-
-
the enzyme processes the 5' ends of tRNA precursors, the substrate population includes over 80 different competing ptRNAs in Escherichia coli, sequence and secondary structure of representative ptRNAs, overview. Its mode of molecular recognition differs from other catalytic RNAs in two important ways. First, its biological role in ptRNA processing requires that it act in trans as a multiple turnover enzyme, whereas other ribozymes, with the exceptions of the ribosome and spliceosome, undergo single turnover self-splicing or self-cleavage reactions. Second, RNase P processes multiple RNA substrates, including all ptRNAs in the cell, whereas other ribozymes, again with the exceptions of the ribosome and spliceosome, have one specific substrate
-
-
-
additional information
?
-
-
the enzyme processes the 5'-end of tRNAs
-
-
-
additional information
?
-
L0N807
the enzyme processes the 5'-end of tRNAs
-
-
-
additional information
?
-
-
the mechanism by which the enzyme processes the valU and lysT polycistronic transcripts (valV valW, valU valX, valY lysY and lysT valT lysW valZ lysY lysZ lysQ) involves initiation of processing by first endonucleolytically removing the Rho-independent transcription terminators from the primary valU and lysT transcripts. Subsequently, the enzyme proceeds in the 3' -> 5' direction generating one pre-tRNA at a time. Identification of cleavage sites using RNA circularization, overview
-
-
-
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
-
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
-
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
-
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
-
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
-
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
-
additional information
?
-
-
the natural substrate is precursor tRNA. Proteinaceous PRORP1 catalyzes all of the other noncanonical, yet vital functions of nuclear yeast RNase P, which may include processing of non-canonical RNAs
-
-
-
additional information
?
-
Escherichia coli MG1693
-
the mechanism by which the enzyme processes the valU and lysT polycistronic transcripts (valV valW, valU valX, valY lysY and lysT valT lysW valZ lysY lysZ lysQ) involves initiation of processing by first endonucleolytically removing the Rho-independent transcription terminators from the primary valU and lysT transcripts. Subsequently, the enzyme proceeds in the 3' -> 5' direction generating one pre-tRNA at a time. Identification of cleavage sites using RNA circularization, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the protein component C5 acts as a cofactor for the catalytic M1 RNA subunit that processes the 5' leader sequence of precursor tRNA. Rpp29, a conserved protein subunit of human RNase P, can substitute for C5 protein in reconstitution assay of M1 RNA activity. Distinct protein folds in two unrelated protein cofactors can facilitate transition from RNA-based to ribonucleoprotein-based catalysis by RNase P
-
additional information
-
RNase P RNA is capable of cleaving its substrate in vitro in the absence of any protein cofactor
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
Mg2+, Ca2+, Sr2+, and, to a lesser extent, Mn2+ can perform the electrostatic shielding function and preserve the structural properties of the two RNA molecules necessary to keep the substrate and enzyme in appropriate conformations
Ca2+
-
suppresses enzyme activity, but supports RNA folding and substrate binding, used for binding assays
Ca2+
-
much less efficiently than Mg2+ or Mn2+
Ca2+
-
Ca2+ can replace Mg2+
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+
-
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+
-
presence of the protein cofactor increases and equalized substrate affinity and abolishes the substrate affinity differences seen for Escherichia coli relative to Bacillus subtilis P RNA
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+
-
activates; metal-stabilized conformational change in RNase P that accompanies substrate binding and is essential for efficient catalysis
Cd2+
-
changes the cleavage pattern
Cs+
-
less effective in activation than K+
Cs+
-
supports activity at 100-200 mM
Cu2+
-
changes the cleavage pattern
K+
-
optimal activity at 0.3-1 M NH4Cl or KCl
K+
-
monovalent cation required: Na+, K+ or NH4+
K+
-
maximal activity at 0.1-0.2 M
K+
-
monovalent cation required, K+ is most effective
K+
-
optimal activity at 150-200 mM KCl
K+
-
optimal concentration 40-60 mM
K+
-
optimal activity in presence of 5 mM KCl or 10 mM NH4Cl
K+
-
stimulates at less than 30 mM
KCl
-
activates, best at 200 mM
Li+
-
less effective in activation than K+
Mg2+
-
can substitute for the C5 protein as a cofactor, since M1 RNA alone can carry out the catalytic reaction in the buffer that contains more than 20 mM Mg2+; required
Mg2+
-
strict requirement for a divalent cation, Mg2+ or Mn2+. Hexacoordinated Mg2+ binds to the catalytic site on M1 RNA
Mg2+
-
optimal activity at 20-200 mM MgCl2
Mg2+
-
-
Mg2+
-
Mg2+, Ca2+, Sr2+, and, to a lesser extent, Mn2+ can perform the electrostatic shielding function and preserve the structural properties of the two RNA molecules necessary to keep the substrate and enzyme in appropriate conformations; the only metal ion that can act as cofactor for activity of M1 RNA
Mg2+
-
optimal concentration: 60-90 mM
Mg2+
-
5-10 mM required
Mg2+
-
optimal activity at 5 mM; required
Mg2+
-
required for efficient cleavage at the correct position. Essential for the folding of the active conformation of RNase P RNA
Mg2+
-
required at a concentration of at least 2 mM
Mg2+
-
required
Mg2+
-
optimal concentration is 55 mM
Mg2+
-
optimal activity at 1 mM MgCl2
Mg2+
-
the RNA subunit requires 20 mM Mg2+ for optimal activity
Mg2+
-
10-15 mM required for optimal activity
Mg2+
-
optimal activity in presence of 5 mM MgCl2
Mg2+
-
maximally active at 2.5-30 mM MgCl2
Mg2+
-
is the most effective cofactor, can be replaced by Mn2+
Mg2+
-
optimal concentration for RNase P RNA activity is 250 mM MgCl2
Mg2+
-
dependent on, optimal at 2-10 mM
Mg2+
-
dependent on, at least half-maximal activity between 8-80 mM
Mg2+
-
required for hyperprocessing reaction, at about 10 mM
Mg2+
-
absolutely required, optimal at about 20 mM, for catalysis and substrate shape recognition, influences substrate binding affinity
Mg2+
-
absolutely required, optimal at about 10 mM, for catalysis and substrate shape recognition, influences substrate binding affinity
Mg2+
-
potential catalytic transition state structure including 3 required divalent metal ions, coordinated to nonbinding phosphate group oxygens
Mg2+
-
interaction with the helix P4
Mg2+
-
coordination to nucleotide A67 of the enzymes RNA
Mg2+
-
high activation
Mg2+
-
high activation, specific for
Mg2+
-
best metal ion, required for folding of the RNA, for binding of protein and substrate, and for catalytic activity
Mg2+
-
required, optimal cleavage at 20 mM for the reconstituted mini-enzyme, reduced activity at 40-100 mM, the wild-type enzyme shows no activity at 100 mM
Mg2+
-
optimal at 5-10 mM for the holoenzyme, the RNA subunit alone is active only at 100 mM MgCl2
Mg2+
-
dependent on, binds to the pro-Rp nonbridging oxygen of the scissile bond, coordination
Mg2+
-
replacement, deletion, or insertion (except at G63G64) of bases of the J3/4 domain of Escherichia coli ribonuclease P, can be compensated for by the presence of a high concentration of magnesium ions above 20 mM
Mg2+
-
optimally at 7.5 mM
Mg2+
-
optimal 120 mM; optimal 120 mM RNase P RNA + RNase P protein 21 + RNase P protein 29; optimal 30 mM; optimal 500 mM
Mg2+
-
essential
Mg2+
-
dependent on, the optimum is at 5 mM MgCl2, when reactions are carried out at pH 7.5 and 37C
Mg2+
-
enzymatic activity depends on the presence of divalent metal ions such as Mg2+
Mg2+
-
essential for activity, the ribozyme prefers the wild type pre-tRNA (A7) substrate at low Mg2+
Mg2+
-
required for activity
Mg2+
-
dependent on
Mg2+
-
required for folding, substrate binding, and catalysis
Mg2+
-
required for formation of the Pop6-Pop7-RNA complex
Mg2+
-
assay buffer
Mg2+
-
required for activation
Mg2+
-
60 mM is optimal for the holoenzyme
Mg2+
-
10 mM is optimal for the holoenzyme
Mg2+
-
mitochondrial RNase P requires divalent metal ions, preferably Mg2+, for cleavage
Mg2+
-
required for catalysis
Mg2+
-
for the LNA variant, parallel pathways leading to cleavage at the c0 and m+1 sites have different pH profiles, with a higher Mg2+ requirement for c0 versus m+1 cleavage. The strong catalytic defect for LNA and 2'-OCH3 supports a model where the extra methylene (LNA) or methyl group (2'-OCH3) causes a steric interference with a nearby bound catalytic Mg2+ during its recoordination on the way to the transition state for cleavage. Presence of the protein cofactor suppresses the ground state binding defects, but not the catalytic defects
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+
-
required
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+
Q00XA5
required
Mg2+
-
required
Mg2+
Pyrobaculum sp.
-
required
Mg2+
-
metal-stabilized conformational change in RNase P that accompanies substrate binding and is essential for efficient catalysis
Mg2+
-
the bulge stem-loop structure containing J3/4 and helix P4 is involved in the interaction with Mg2+ ions important for catalysis
Mg2+
-
required, the requirement of Mg2+ for catalysis varies with the substrate. Deletion of the S-domain changes the Mg2+ requirement
Mg2+
-
required
Mg2+
Q9X1H4
required, the active site includes at least two metal ions, RNA U52 nucleotide binds a metal ion at the active site
Mn2+
-
can promote catalysis
Mn2+
-
-
Mn2+
-
strict requirement for a divalent cation, Mg2+ or Mn2+
Mn2+
-
Mg2+, Ca2+, Sr2+, and, to a lesser extent, Mn2+ can perform the electrostatic shielding function and preserve the structural properties of the two RNA molecules necessary to keep the substrate and enzyme in appropriate conformations
Mn2+
-
effectively substitutes for Mg2+
Mn2+
-
Mn2+ can replace for Mg2+ in activation
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+
-
rescues A67Rp- and A67Sp-phosphorothionate modified inactive enzyme at 5 mM completely and partially, respectively
Mn2+
-
can substitute for Mg2+, slightly lower activity
Mn2+
-
Mn2+ can replace Mg2+
Na+
-
monovalent cation required: Na+, K+ or NH4+
Na+
-
less effective in activation than K+
Na+
-
less effective in activation than K+
Na+
-
supports activity at 100-200 mM
NaCl
-
activates
NaCl
-
activates, best at 50 mM
NH4+
-
optimal activity at 0.3-1 M NH4Cl or KCl
NH4+
-
-
NH4+
-
stimulates activity of M1 RNA
NH4+
-
optimal concentration: 100-200 mM
NH4+
-
monovalent cation required: Na+, K+ or NH4+. Optimal NH4+ concentration is 200 mM
NH4+
-
monovalent cation required, NH4+ is less effective than K+
NH4+
-
supports activity at 300 mM
NH4+
-
800 mM NH4Cl is required for optimal activity. (NH4)2SO4 is significantly more active than NH4Cl
NH4+
-
optimal concentration: 40-60 mM
NH4+
-
optimal activity in presence of 5 mM KCl or 10 mM NH4Cl
NH4+
-
optimal concentration for RNase P RNA activity is 3 M NH4Cl
NH4+
-
dependent on, the optimum is at 70 mM NH4Cl, when reactions are carried out at pH 7.5 and 37C
NH4Cl
-
activates, best at 200-400 mM
Ni2+
-
changes the cleavage pattern
Pb2+
-
Pb2+ can replace Mg2+
Sr2+
-
Mg2+, Ca2+, Sr2+, and, to a lesser extent, Mn2+ can perform the electrostatic shielding function and preserve the structural properties of the two RNA molecules necessary to keep the substrate and enzyme in appropriate conformations
Zn2+
-
Zn2+ can replace Mg2+
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
Zn2+
-
bound by conserved residues. A putative zinc-finger-like structure is split in two separate motifs. The first motif (CxxC) contains two conserved cysteines upstream of the NYN domain at positions 344 and 347 for PRORP1, whereas the second motif involves a conserved histidine and a cysteine, downstream of the NYN domain, at positions 548 and 565, respectively. The downstream conserved motif has a stronger affinity for the metal than the upstream CxxC coordination element
Mn2+
-
Mn2+ paramagnetic line broadening experiments reveal strong metal localization at residues corresponding to G378 and G379
additional information
-
requires a monovalent and a divalent cation for activity
additional information
-
requires a monovalent and a divalent cation for activity
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
-
divalent metal ions are important cofactors for the reaction
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
additional information
-
divalent metal ions are important cofactors for the reaction
additional information
-
optimal ionic strength at 800 mM ammonium acetate at 60C
additional information
-
at least half-maximal activity at 1 M ammonium acetate
additional information
-
divalent metal cations are essential for catalysis and stabilize the enzyme conformation and subunit interaction
additional information
-
at least 2 metal ions per enzyme molecule, one catalytically and one structurally important, interactions of divalent metal cations at the pro-Rp and ProSp non-bridging phosphate oxygens with nucleotide A67 in the universally conserved helix p4 are essential for the folding and function of the enzymes' catalytic RNA component, interaction kinetics
additional information
-
divalent metal cations are essential
additional information
-
divalent metal ions are absolutely required, reduced activity with Ca2+
additional information
-
enzyme is dependent on divalent metal ions, enzyme contains a metal binding loop
additional information
-
enzyme is dependent on divalent metal ions
additional information
-
enzyme is dependent on divalent metal ions, enzyme contains a metal binding loop
additional information
-
Ca2+ and Mn2+ cannot substitute for Mg2+
additional information
-
Mg2+ is not required for activity
additional information
-
Mn2+, Co2+, Ni2+, Cu2+, Au3+, Pb2+, La3+, Pr3+, Sm3+, Gd3+, Dy3+, Yb3+, and Lu3+ are able to bind to RNase P but are not specific proxies for Mg2+
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+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
all-trans-retinoic acid
-
-
aminoglycosides
-
inhibition by displacing functionally important Mg2+ ions
-
ATP
-
above 2 mM, progressively inhibitory
Ca2+
-
suppresses enzyme activity, but supports RNA folding and substrate binding, used for binding assays
calcipotriol
-
-
DNA 14-mer
-
-
-
EDTA
-
inhibits hyperprocessing reaction
EDTA
-
inactivation
EDTA
-
inactivation
guide DNA
-
complete inhibition at 0.005 mM
-
hexa-D-arginine-neomycin conjugate
-
-
isotretinoin
-
13-cis-retinoic acid
K+
-
above 100 mM
locked nucleic acid 14-mer
-
-
-
Mg2+
-
above 100 mM
Mg2+
-
above 40 mM
Mg2+
-
inhibited at concentrations greater than 7.5 mM
micrococcal nuclease
-
-
-
N1,N12-bis(all-trans-retinoyl)spermine
-
-
N1,N12-bisacitretinylspermine
-
-
N1-(all-trans-retinoyl)spermine
-
-
N1-acitretinylspermine
-
-
N4,N9-bis(all-trans-retinoyl)spermine
-
-
NaCl
-
inhibition of the reconstituted mini-enzyme at 0.4 M NaCl
NeoG6
-
N,N'''-[(1R,3S,4R,5R,6S)-4-[(2,6-dicarbamimidamido-2,6-dideoxy-alpha-D-glucopyranosyl)oxy]-5-[[3-O-(2,6-dicarbamimidamido-2,6-dideoxy-beta-L-idopyranosyl)-beta-D-ribofuranosyl]oxy]-6-hydroxycyclohexane-1,3-diyl]diguanidine
NeoK6
-
D-streptamine, O-2,6-dideoxy-2,6-bis[[(2S)-2,6-diamino-1-oxohexyl]amino]-beta-L-idopyranosyl-(1-3)-O-beta-D-ribofuranosyl-(1-5)-O-[2,6-dideoxy-2,6-bis[[(2S)-2,6-diamino-1-oxohexyl]amino]-alpha-D-glucopyranosyl-(1-4)]-2-deoxy-N1,N3-bis[(2S)-2,6-diamino-1-oxohexyl]-
neomycin B
-
-
neomycin B
-
the inhibition is of non-competitive type, increasing Mg2+ concentrations from 3 to 20 mM, at a constant neomycin concentration (0.05 mM), result in a considerable recovery of the activity (about 40%)
neomycinB
-
-
NeoR5
-
D-streptamine, O-2,6-bis[[(2S)-2-amino-5-[(aminoiminomethyl)amino]-1-oxopentyl]amino]-2,6-dideoxy-beta-L-idopyranosyl-(1-3)-O-beta-D-ribofuranosyl-(1-5)-O-[2,6-bis[[(2S)-2-amino-5-[(aminoiminomethyl)amino]-1-oxopentyl]amino]-2,6-dideoxy-alpha-D-glucopyranosyl-(1-4)]-N1-[(2S)-2-amino-5-[(aminoiminomethyl)amino]-1-oxopentyl]-2-deoxy-
NeoR5
-
D-streptamine, O-2,6-bis[[(2S)-2-amino-5-[(aminoiminomethyl)amino]-1-oxopentyl]amino]-2,6-dideoxy-beta-L-idopyranosyl-(1-3)-O-beta-D-ribofuranosyl-(1-5)-O-[2,6-bis[[(2S)-2-amino-5-[(aminoiminomethyl)amino]-1-oxopentyl]amino]-2,6-dideoxy-alpha-D-glucopyranosyl-(1-4)]-N1-[(2S)-2-amino-5-[(aminoiminomethyl)amino]-1-oxopentyl]-2-deoxy- (NeoR5), Methanothermobacter thermautotrophicus RNase P is inhibited quite significantly and progressively up to 10 microM NeoR5
NeoR5
-
NeoR5
NH4+
-
above 100 mM
NH4+
-
inhibited at ammonium concentrations greater than 100 mM in the presence of 7.5 mM MgC12
nona-D-arginine-neamine conjugate
-
-
nona-D-arginine-neomycin conjugate
-
-
paromomycin
-
-
peptide nucleic acid 14-mer
-
-
-
peptide nucleic acid 14-mer
-
PNA
-
phosphorothionate
-
modifies nucleotides A67Rp and A67Sp, no remaining activity with Mg2+, complete rescue of activity with 5 mM Mn2+ for A67Rp, partially 65fold for A67Sp
phosphorothionate
-
inhibition of activity due to phosphothionate substitution at the pro-Rp or pro-Sp nonbridging position of the scissile bond in tRNA, activity cannot be recovered by Mn2+
poly(U) RNA
-
binding and structure analysis, overview
-
proteinase K
-
-
-
puromycin
-
-
puromycin
-
in millimolar range
puromycin
-
about 80% inhibition at 6 mM
retinoic acid
-
-
RNA
-
5S RNA or a mixture of 16S and 23S rRNA
tRNA
-
mature tRNA is a competitive inhibitor of pre-tRNA cleavage
tRNA
-
bulk tRNA
unstructured, single-stranded RNA
-
inhibits RNase P in a size-dependent manner, binding and structure analysis, overview
-
Zn2+
-
results in misscleavage of te substrate at 1-5 mM
mixed-sequence RNAs
-
only a small fraction of the mixed-sequence RNA is cleaved by RNase P
-
additional information
-
substitution of the pro-Rp nonbridging oxygen with sulfur at the scissile bond does not inhibit the enzyme
-
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
-
disruption of tertiary structure inhibits the enzyme
-
additional information
-
no inhibition by phosphothionate
-
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
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-methyl-2,4-pentanediol
-
enhances cleavage reaction of the M1 RNA subunit alone
PhoPop5 protein
-
PhoPop5 is an archaeal homolog of human RNase P protein hPop5 involved in the activation of RNase P RNA in the hyperthermophilic archaeon Pyrococcus horikoshii. Extra-structural elements in the RNA recognition motif in PhoPop5 play a crucial role in the activation, that is, the C-terminal extension in the dimerized PhoPop5 protein through the loop between alpha1 and alpha2 is essential for the activation of the enzyme by promoting RNA annealing and RNA strand displacement
-
Polyethylene glycol
-
enhances cleavage reaction of the M1 RNA subunit alone
roxithromycin
-
-
spermidine
-
M1 RNA subunit can catalyze the cleavage of tRNA precursor molecules in the presence of 5 mM spermine or spermidine
spermidine
-
2.5 mM increases activity by 2-4fold in presence of 5 mM MgCl2
spermine
-
M1 RNA subunit can catalyze the cleavage of tRNA precursor molecules in the presence of 5 mM spermine or spermidine
spermine
-
A 2-fold increase in enzyme activity is observed when 1.25 mM spermine is included in the reaction mixture.
spiramycin
-
most potent activator
tylosin
-
-
erythromycin
-
-
additional information
-
enzyme requires low salt levels
-
additional information
-
enzyme requires very high salt levels
-
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
-
additional information
P62426 and P60780 and P60781 and P60832 and P62378
ribosomal protein L7Ae is a subunit of archaeal RNase P. Addition of L7Ae to this RNase P complex increases the optimal reaction temperature and kcat/Km (by approximately 360fold) for pre-tRNA cleavage to those observed with partially purified native enzyme
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000063
human pre-tRNATyr
-
pH 7.6, 37C
-
0.000072
human pre-tRNATyr
-
pH 8.0, 37C, 20 mM Mg2+
-
0.00025
human pre-tRNATyr
-
pH 8.0, 37C, 40 mM Mg2+
-
0.00043
human pre-tRNATyr
-
pH 8.0, 37C, 20 mM Mg2+
-
0.000016
pre-tRNA
-
-
-
0.00024
pre-tRNA supS1 tRNASer
-
-
-
0.00006
pre-tRNA-Tyr
-
pre-tRNA-Tyr without the 3'-UUUUU trailer, at 25C, pH 8.0, in 10 mM HEPES buffer with 10 mM MgCl2 and 100 mM KCl
-
0.0001
pre-tRNA-Tyr
-
pre-tRNA-Tyr with the 3'-UUUUU trailer, at 25C, pH 8.0, in 10 mM HEPES buffer with 10 mM MgCl2 and 100 mM KCl
-
0.00004
pre-tRNAAsp
-
-
-
0.00011
pre-tRNAAsp
-
catalyzed by RNase P RNA
-
0.00022
pre-tRNAAsp
-
catalyzed by circular RNase P RNA
-
32
pre-tRNAAsp
-
-
-
0.00000009
pre-tRNATyr
-
wild-type enzyme, pH not specified in the publication, 65C
-
0.000009
pre-tRNATyr
-
-
-
0.000044
pre-tRNATyr
P62426 and P60780 and P60781 and P60832 and P62378
37C, pH 7.5, in the presence of L7Ae
-
0.0017
pre-tRNATyr
-
from E. coli, RNase P RNA
-
0.0026
pre-tRNATyr
P62426 and P60780 and P60781 and P60832 and P62378
37C, pH 7.5, in the absence of L7Ae
-
0.00018
ptRNATyr
-
from Escherichia coli, enzyme subunit RNase P RNA + Pop5 + RNase P protein 30 + RNase P protein 21 + RNase P protein 29
-
0.00653
ptRNATyr
-
enzyme subunit RNase P RNA + RNase P protein 21 + RNase P protein 29
-
0.0116
ptRNATyr
-
from Escherichia coli, emzyme subunit RNase P RNA + Pop5 + RNase P protein 30
-
0.0305
ptRNATyr
-
from Escherichia coli, enzyme substrate Rnase P RNA
-
0.000244
SupS1 precursor
-
in 50 mM Tris /HCl pH 7.5, 100 mM NH4Cl, 5 mM MgCl2, 2.5 mM EGTA and 0.5 U Rnasin
-
0.00025
tRNA
-
pH 7.5, 77C
0.00002
tRNA precursor
-
derived from the sup S1 and sup3-e tRNASer genes of Schizosaccharomyces pombe
0.0000345
tRNA precursor
-
pH 8.0, 65C, in presence of 800 mM ammonium acetate and 5 mM MgCl2
0.000055
tRNA precursor
-
nuclear enzyme form
0.0000684
tRNA precursor
-
pH 8.0, 50C, in presence of 50 mM ammonium acetate and 30 mM MgCl2
0.000012
tRNAPhe (G+1) precursor
-
37C, substrate substituted with phosphothionate from GMPaS
-
0.000016
tRNAPhe (G+1) precursor
-
37C
-
0.00001
tRNATyr
-
-
0.0002
tRNATyr
-
-
0.000223
tRNATyr precursor
-
pH 7.5, 50C, enzyme RNA subunit
-
0.00054
human pre-tRNATyr
-
pH 8.0, 37C, 40 mM Mg2+
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetics, the rate constant for the scissile bond cleavage is pH-dependent
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
both pre-steady state and steady state kinetics
-
additional information
additional information
-
pre-steady state kinetics, nuclear enzyme form
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
-
-
additional information
additional information
-
KM-values for pre-tRNATyr, mutant enzymes
-
additional information
additional information
-
kinetics of deletion mutants
-
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); the RNR motif enhances the affinity of RNase P for pre-tRNA
-
additional information
additional information
-
Michaelis-Menten steady-state reaction kinetics of two tRNA precursors showing fast substrate cleavage relative to dissociation, and competitive substrate kinetics of the enzyme, overview. Reactions containing two or more ptRNAs follow simple competitive alternative substrate kinetics in which the relative rates of processing are determined by ptRNA concentration and their V/K. Rates of ptRNA processing by RNase P are tuned for uniform specificity and consequently optimal coupling to precursor biosynthesis. Multiple turnover reactions and competitive multiple turnover reactions, detailed overview
-
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
-
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, pseudo-first-order rate constants of cleavage are calculated by nonlinear regression analysis
-
additional information
additional information
Q9X1H4
Michaelis-Menten single-turnover reaction kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000011
human pre-tRNATyr
-
pH 8.0, 37C, 20 mM Mg2+
-
0.00002
human pre-tRNATyr
-
pH 8.0, 37C, 20 mM Mg2+
-
0.00004
human pre-tRNATyr
-
pH 8.0, 37C, 40 mM Mg2+
-
0.000056
human pre-tRNATyr
-
pH 8.0, 37C, 40 mM Mg2+
-
0.07
pre-tRNA
-
absence of spiramycin
-
0.18
pre-tRNA
-
presence of spiramycin
-
0.077
pre-tRNA-Tyr
-
pre-tRNA-Tyr without the 3'-UUUUU trailer, at 20C, pH 8.0, in 10 mM HEPES buffer with 10 mM MgCl2 and 100 mM KCl
-
0.08
pre-tRNA-Tyr
-
pre-tRNA-Tyr with the 3'-UUUUU trailer, at 20C, pH 8.0, in 10 mM HEPES buffer with 10 mM MgCl2 and 100 mM KCl
-
0.02
pre-tRNAAsp
-
catalyzed by RNase P RNA
-
0.09
pre-tRNAAsp
-
catalyzed by circular RNnase P RNA
-
0.009
pre-tRNATyr
-
wild-type enzyme, pH not specified in the publication, 65C
-
0.107
pre-tRNATyr
-
from E. coli, RNase P RNA
-
0.17
pre-tRNATyr
P62426 and P60780 and P60781 and P60832 and P62378
37C, pH 7.5, in the absence of L7Ae
-
1.05
pre-tRNATyr
P62426 and P60780 and P60781 and P60832 and P62378
37C, pH 7.5, in the presence of L7Ae
-
1.3
pre-tRNATyr
-
-
-
0.0063
ptRNATyr
-
from Escherichia coli, enzyme substrate Rnase P RNA
-
0.01
ptRNATyr
-
enzyme subunit RNase P RNA + RNase P protein 21 + RNase P protein 29
-
0.1583
ptRNATyr
-
from Escherichia coli, enzyme subunit RNase P RNA + Pop5 + RNase P protein 30 + RNase P protein 21 + RNase P protein 29
-
0.1917
ptRNATyr
-
from Escherichia coli, emzyme subunit RNase P RNA + Pop5 + RNase P protein 30
-
0.57
tRNA precursor
-
pH 8.0, 50C, in presence of 50 mM ammonium acetate and 30 mM MgCl2
0.88
tRNA precursor
-
pH 8.0, 65C, in presence of 800 mM ammonium acetate and 5 mM MgCl2
1.3
tRNA precursor
-
nuclear enzyme form
6
tRNA precursor
-
enzyme RNA moiety, pH 7.0
0.0005
tRNAPhe (G+1) precursor
-
37C, substrate substituted with phosphothionate from GMPaS
-
0.003
tRNAPhe (G+1) precursor
-
37C
-
0.14
tRNATyr precursor
-
pH 7.5, 50C, enzyme RNA subunit
-
0.04
human pre-tRNATyr
-
pH 7.6, 37C
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
KM-values for pre-tRNATyr, mutant enzymes
-
additional information
additional information
-
native RNase P turnover at steady state is limited by product release
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.83
pre-tRNAPhe
Q9X1H4
recombinant mutant R89A/U52C, pH 7.5, 37C
0
1
pre-tRNAPhe
Q9X1H4
recombinant mutant F17A/U52C, pH 7.5, 37C
0
8.3
pre-tRNAPhe
Q9X1H4
recombinant mutant F17A, pH 7.5, 37C
0
10
pre-tRNAPhe
Q9X1H4
recombinant mutant R89A, pH 7.5, 37C
0
13
pre-tRNAPhe
Q9X1H4
recombinant mutant U52C, pH 7.5, 37C
0
28.3
pre-tRNAPhe
Q9X1H4
recombinant mutant F21A, pH 7.5, 37C
0
40
pre-tRNAPhe
Q9X1H4
recombinant mutant K53A, pH 7.5, 37C
0
44.2
pre-tRNAPhe
Q9X1H4
recombinant mutant K90A, pH 7.5, 37C
0
54.2
pre-tRNAPhe
Q9X1H4
recombinant mutant R15A, pH 7.5, 37C
0
65
pre-tRNAPhe
Q9X1H4
recombinant mutant R14A, pH 7.5, 37C
0
66.7
pre-tRNAPhe
Q9X1H4
recombinant mutant K52A, pH 7.5, 37C
0
70
pre-tRNAPhe
Q9X1H4
recombinant mutant K51A, pH 7.5, 37C
0
120
pre-tRNAPhe
Q9X1H4
recombinant mutant R60A, pH 7.5, 37C
0
170
pre-tRNAPhe
Q9X1H4
recombinant mutant K62A, pH 7.5, 37C
0
180
pre-tRNAPhe
Q9X1H4
recombinant wild-type enzyme, pH 7.5, 37C
0
181.7
pre-tRNAPhe
Q9X1H4
recombinant mutant K56A, pH 7.5, 37C
0
198.3
pre-tRNAPhe
Q9X1H4
recombinant mutant R59A, pH 7.5, 37C
0
261.7
pre-tRNAPhe
Q9X1H4
recombinant mutant R65A, pH 7.5, 37C
0
65.4
pre-tRNATyr
P62426 and P60780 and P60781 and P60832 and P62378
37C, pH 7.5, in the absence of L7Ae
0
23860
pre-tRNATyr
P62426 and P60780 and P60781 and P60832 and P62378
37C, pH 7.5, in the presence of L7Ae
0
additional information
additional information
-
a native precursor form of yeast RNase P (RNase P RNA + 7 RNase P proteins, without POP3/RPP38 and Rpr2p/RPP21) displays an identical steady-state rate as the mature form (RNase P RNA + 9 RNase P proteins)
0
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.008
acitretin
-
at 37C, in 50 mM Tris/HCl pH 7.6, 10 mM NH4Cl, 5 mM MgCl2, and 5 mM dithiothreitol
0.015
all-trans-retinoic acid
-
at 37C, in 50 mM Tris/HCl pH 7.6, 10 mM NH4Cl, 5 mM MgCl2, and 5 mM dithiothreitol
2 - 5
DNA 14-mer
-
-
-
0.02
isotretinoin
-
at 37C, in 50 mM Tris/HCl pH 7.6, 10 mM NH4Cl, 5 mM MgCl2, and 5 mM dithiothreitol
3.9
locked nucleic acid 14-mer
-
-
-
0.0005
N1,N12-bis(all-trans-retinoyl)spermine
-
at 37C, in 50 mM Tris/HCl pH 7.6, 10 mM NH4Cl, 5 mM MgCl2, and 5 mM dithiothreitol
0.00095
N1,N12-bisacitretinylspermine
-
at 37C, in 50 mM Tris/HCl pH 7.6, 10 mM NH4Cl, 5 mM MgCl2, and 5 mM dithiothreitol
0.0024
N1-(all-trans-retinoyl)spermine
-
at 37C, in 50 mM Tris/HCl pH 7.6, 10 mM NH4Cl, 5 mM MgCl2, and 5 mM dithiothreitol
0.00245
N1-acitretinylspermine
-
at 37C, in 50 mM Tris/HCl pH 7.6, 10 mM NH4Cl, 5 mM MgCl2, and 5 mM dithiothreitol
0.0011
N4,N9-bis(all-trans-retinoyl)spermine
-
at 37C, in 50 mM Tris/HCl pH 7.6, 10 mM NH4Cl, 5 mM MgCl2, and 5 mM dithiothreitol
0.037
neomycin B
-
in 50 mM Tris /HCl pH 7.5, 100 mM NH4Cl, 5 mM MgCl2, 2.5 mM EGTA and 0.5 U Rnasin
12.5
peptide nucleic acid 14-mer
-
-
-
1.475
retinol
-
at 37C, in 50 mM Tris/HCl pH 7.6, 10 mM NH4Cl, 5 mM MgCl2, and 5 mM dithiothreitol
2.2
RNA 14-mer
-
-
-
4.35
Ro 13-6298
-
at 37C, in 50 mM Tris/HCl pH 7.6, 10 mM NH4Cl, 5 mM MgCl2, and 5 mM dithiothreitol
0.045
Ro 13-7410
-
at 37C, in 50 mM Tris/HCl pH 7.6, 10 mM NH4Cl, 5 mM MgCl2, and 5 mM dithiothreitol
2.8
Ro 15-0778
-
at 37C, in 50 mM Tris/HCl pH 7.6, 10 mM NH4Cl, 5 mM MgCl2, and 5 mM dithiothreitol
3.6
Ro 15-1570
-
at 37C, in 50 mM Tris/HCl pH 7.6, 10 mM NH4Cl, 5 mM MgCl2, and 5 mM dithiothreitol
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.006
NeoG6
-
-
0.003
NeoK6
-
-
0.074
neomycin B
-
in 50 mM Tris /HCl pH 7.5, 100 mM NH4Cl, 5 mM MgCl2, 2.5 mM EGTA and 0.5 U Rnasin
0.4
neomycinB
-
-
0.0005
NeoR5
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
-
assay at
6
-
assay at
6.1
-
assay at
7 - 7.4
-
assay at
7.4 - 7.5
-
assay at
7.4
-
assay at
7.4
-
assay at
7.4
-
assay at
7.5
-
recombinant holoenzyme
7.5
Q00XA5
assay at
7.5
-
assay at
7.5
L0N807
assay at
7.5
-
assay at
7.5
-
assay at
7.6
-
assay at
7.7 - 8.7
-
-
8
-
broad optimum around pH 8.0
8
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8.2
-
pH 7.0: about 30% of maximal activity, pH 8.2: about 45% of maximal activity
7 - 9
-
less than 50% of maximal activity at pH 7.0 and 9.0
7.4 - 8.5
-
pH 7.4: about 50% of maximal activity, pH 8.0-8.5: optimum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28
-
assay at
36 - 38
P62426 and P60780 and P60781 and P60832 and P62378
optimal assay temperature of in vitro reconstituted enzyme in the absence of ribosomal protein L7Ae
37 - 55
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
Q00XA5
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
L0N807
assay at
37
-
assay at
37
-
assay at
37
-
assay at
48 - 50
P62426 and P60780 and P60781 and P60832 and P62378
optimal assay temperature of in vitro reconstituted enzyme in the presence of ribosomal protein L7Ae
50
-
assay at
50
-
about, recombinant holoenzyme
65 - 70
-
wild-type enzyme
70
-
the protein subunit Ph1496p elevates the optimum temperature from 55C (for reconstituted enzyme particles composed of RNase P RNA and four proteins: Ph1481p, Ph1601p, Ph1771p, and Ph1877p) to 70C which is the temperature optimum of the authentic RNase P from pyrococcus horikoshii AT3
77
-
The temperature optimum for the reaction is 77 C, reflecting the thermophilic character of the organism
additional information
-
optimal growth temperature of Thermotoga maritima is about 80C
additional information
-
the deletion mutants show a slightly reduced optimal temperature compared to the wild-type enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 42
-
25C: about 60% of maximal activity, 42C: about 25% of maximal activity
70 - 80
-
and above, 50% activity at about 70C
additional information
-
no activity at 65C and above, recombinant holoenzyme
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.6 - 4.7
-
protein subunits Pop1p, Pop3p, Pop4p, Pop6p, Pop7p, Rpp1p, and Rpr2p
4.6 - 4.7
-
protein subunit Rpp20; protein subunit Rpp30
4.9
-
protein subunit Pop8p
4.9
-
protein subunit Rpp40
5.5
-
protein subunit Rpp25; protein subunit Rpp29; protein subunits Pop1, Rpp21 and Rpp38
6.9
-
protein subunit Pop5p
6.9
-
protein subunit Pop5; protein subunit Rpp14
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
contains protein subunits Rpp29 and Rpp38
Manually annotated by BRENDA team
-
enzyme form might be RNA-independent
Manually annotated by BRENDA team
-
RNA subunit H1
Manually annotated by BRENDA team
-
all putative components of the enzyme are encoded by the nucleus
Manually annotated by BRENDA team
-
mitochondrial enzyme form of RNase MRP
Manually annotated by BRENDA team
-
mitochondrial ribozyme form
Manually annotated by BRENDA team
-
RNases P and MRP
Manually annotated by BRENDA team
-
RNases P and MRP, enzyme consists of RNA component Rpm1r and protein component Rpm2p, the latter is required for the processing of the first
Manually annotated by BRENDA team
-
the RNA subunits of the mitochondrial and nuclear enzymes are identical
Manually annotated by BRENDA team
-
the enzyme is composed of two proteins, protein PRORP2 is localized to the branched trypanosomatid mitochondrion and has a cleavable N-terminal targeting sequence
Manually annotated by BRENDA team
-
nucleolar enzyme form of RNase MRP
Manually annotated by BRENDA team
-
RNase P, all subunits
Manually annotated by BRENDA team
-
the enzyme is composed of a catalytic RNA and two proteins, protein PRORP1 is largely confined to the single central nucleolus of the nuclei and only weak in the nucleoplasm
Manually annotated by BRENDA team
-
nuclear ribozyme form RNase P in nucleoplasm
Manually annotated by BRENDA team
-
nuclear ribozyme forms MPR and P
Manually annotated by BRENDA team
-
nucleoplasm, RNase P, all subunits
Manually annotated by BRENDA team
-
the RNA subunits of the mitochondrial and nuclear enzymes are identical
Manually annotated by BRENDA team
Q00XA5
a nuclear-encoded bacterial RNase P protein homologue
Manually annotated by BRENDA team
-
PRORP2 and PRORP3 are two paralogues of PRORP1
Manually annotated by BRENDA team
Saccharomyces cerevisiae SCWY10
-
-
-
Manually annotated by BRENDA team
Ostreococcus tauri RCC745
-
a nuclear-encoded bacterial RNase P protein homologue
-
Manually annotated by BRENDA team
Escherichia coli MRE, Escherichia coli MRE600
-
-
-
Manually annotated by BRENDA team
Escherichia coli MG1693
-
-
-
Manually annotated by BRENDA team
additional information
-
eukaryotic cells may contain multiple RNase P activities, a nucear type as well as enzyme species in mitochondria and chloroplasts
-
Manually annotated by BRENDA team
additional information
-
not detectable in nucleoplasm
-
Manually annotated by BRENDA team
additional information
-
subcellular localization of different enzyme forms
-
Manually annotated by BRENDA team
additional information
-
in plants, the localization of PRORP1 in chloroplast and mitochondria differs from PRORP2 and 3 in the nucleus
-
Manually annotated by BRENDA team
additional information
-
the chloroplast and mitochondrial genomes of Ostreococcus tauri encode distinct individual RNase P RNA genes and the nucleus encodes both a bacterial-like RNase P protein component, and a proteinaceous RNase P enzyme
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Escherichia coli (strain K12)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
13000
-
P protein plus 400 nt RNA subunit
682171
15400
-
mutant Rpp25(25-170), gel filtration
710148
20600
-
mutant Rpp25, gel filtration
710148
20700
-
mutant Rpp25(25-170), sequence analysis
710148
26000
-
MRPP2
709859
26400
-
mutant HisRpp20(35-140), gel filtration
710148
28100
-
mutant Rpp20(16-140), gel filtration
710148
28600
-
mutant Rpp20(35-140)/Rpp25(25-170), gel filtration
710148
31100
-
mutant Rpp20(35-140)/Rpp25(25-170), sequence analysis
710148
31500
-
mutant Rpp20/Rpp25(25-170), gel filtration
710148
32100
-
full-length Rpp20, gel filtration
710148
36600
-
mutant Rpp20/Rpp25, gel filtration
710148
39200
-
mutant Rpp25, sequence analysis
710148
39900
-
mutant HisRpp20(35-140), sequence analysis
710148
41100
-
mutant Rpp20/Rpp25(25-170), sequence analysis
710148
44400
-
mutant [Rpp20(35-140)-Rpp25(25-170)]/P3 RNA, gel filtration
710148
45000
-
about, gel filtration
654918
45300
-
mutant Rpp20(16-140), sequence analysis
710148
47000
-
full-length Rpp20, sequence analysis
710148
52500
-
mutant [Rpp20-Rpp25]/P3 RNA, gel filtration
710148
53800
-
mutant Rpp20/Rpp25, sequence analysis
710148
56400
-
mutant [Rpp20(35-140)-Rpp25(25-170)]/P3 RNA, sequence analysis
710148
70000
-
gel filtration, mitochondrial enzyme form
656743
70000
-
-
729548
71400
-
mutant [Rpp20-Rpp25]/P3 RNA, sequence analysis
710148
105000
-
mitochondrial enzyme
656107
170000
-
rate-zonal sedimentation in linear isokinetic glycerol gradients
134462
232000
-
glycerol density gradient sedimentation
134456
260000
-
gel filtration
134430
263000
-
gel filtration
134451
400000
-
greater than, gel filtration
134459
400000
-
gel filtration
654918
400000
-
gel exclusion chromatography
680594
440000
-
gel filtration
134456
580000
-
glycerol density gradient sedimentation analysis, gel filtration
134457
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 17500, SDS-PAGE
?
-
x * 18000, recombinant His6-tagged protein StPop5, SDS-PAGE, x * 33000, recombinant His6-tagged protein StRpp25, SDS-PAGE
?
L0N807
x * 21500, AtPop1 protein, two spliced exons encoding a 190 residues long protein, starting from AUG1 from gene At2G47290, SDS-PAGE
decamer
-
1 * 120000, RNA subunit, + 1 * 100500, protein subunit Pop1p, + 1 * 22600, protein subunit Pop3p, 1 * 32900, protein subunit Pop4p, + 1 * 19600, protein subunit Pop5p, + 1 * 18200, protein subunit Pop6p, + 1 * 15800, protein subunit Pop7p, + 1 * 15500, protein subunit Pop8p, + 1 * 32200, protein subunit Rpp1p, + 1 * 16300, protein subunit Rpr2p, or 1 * 112000, RNA subunit NME1, + 1 * 22500, protein subunit SNM1
dimer
-
1 * 13800 + 1 * ?, the enzyme is composed of an RNA called M1 which is 377 nucleotides long and a very basic protein of 13800 Da, called C5. Both subunits are present in the molar ratio 1:1
dimer
-
x * 13990-14000, protein subunit, + x * ?, RNA subunit, SDS-PAGE and mass spectrometry
heterodimer
-
Rpp20 and Rpp25, ITC-200 microcalorimeter experiments
homodimer
-
2 * 16000, full-length Rpp20, gel filtration. 2 * 14100, Rpp20(16-140), gel filtration. 2 * 13200, HisRpp20(35-140), gel filtration
octamer
-
1 * 19000, + 1 * 21000, + 1 * 30000, + 1 * 33000, + 1 * 45000, + 1 * 85000, + 1 * 125000, polypeptides, + 1 * ?, RNA component, SDS-PAGE
octamer
-
1 * 55000 + 1 * 41000, + 1 * 40000, + 1 * 26000, 1 * 24000, + 1 * 18000, + 1 * 16000, polypeptides, + 1 * 76000, RNA subunit, the enzyme is composed of seven polypeptides and an RNA moiety, the RNA component affects significantly the hydrodynamic properties of the RNase P enzyme, resulting in overestimation of the size of the ribonucleoprotein in gel filtration, SDS-PAGE
oligomer
-
1 * 115000, protein subunit Pop1, + 1 * 40000, protein subunit Rpp40, + 1 * 38000, protein subunit Rpp38, + 1 * 30000, protein subunit Rpp30 or Rpp1, + 1 * 29000, protein subunit Rpp29 or Pop4, + 1 * 25000, protein subunit Rpp25, + 1 * 21000, protein subunit Rpp21 or Rpr2, + 1 * 20000, protein subunit Rpp20 or Pop7 or Rpp2, + 1 * 14000, protein subunit Rpp14, + 1 * 105000, RNA subunit H1
oligomer
-
enzyme is composed of 1 RNA subunit H1 and at least 9 protein subunits, namely Rpp14, Rpp20, Rpp21, Rpp29 i.e. Pop4, Rpp30, Rpp40, Pop1, Pop5, and Rpp25
oligomer
-
subunit composition and interaction, 1 essential RNA subunit, i.e. H1 for RNase P or 7-2 for RNase MRP, plus 9 protein components namely Pop1p, Rpp29p, Rpp20p, Rpp30p, Rep38p, Rpp40p, Rpp25p, and Rpp14p for RNase P, or pls 4 protein components namely Pop1p, Rpp29p, Rpp20p, and Rpp30p for RNase MRP, overview
oligomer
-
subunit composition, 1 RNA subunit, i.e. H1 for RNase P or 7-2 for RNase MRP, plus 9 protein components namely Pop1p, Rpp29p, Rpp20p, Rpp30p, Rep38p, Rpp40p, Rpp25p, and Rpp14p for RNase P, or pls 4 protein components namely Pop1p, Rpp29p, Rpp20p, and Rpp30p for RNase MRP, overview
oligomer
-
the nuclear RNase P complex has 1 RNA subunit and 9 distinct protein subunits essential for cell viability and tRNA processing, RNase MRP contains 8 protein subunit and 1 RNA subunit
oligomer
-
a multi-subunit catalytic ribonucleoprotein complex. Step-wise, Mg2+-dependent reconstitutions of Pfu RNaseP with its catalytic RNA subunit and two interacting protein cofactor pairs (RPP21/RPP29 and POP5/RPP30) reveals functional RNP intermediates en route to the RNaseP enzyme 1:1 composition for all subunits when either one or both protein complexes bind the cognate RNA
oligomer
-
the archaeal holoenzyme is associated with 1 RNase P RNA and at least 4 RNase P proteins (POP5, RPP30, RPP21 and RPP29). Archaeal RNase P proteins function as two binary RNase P protein complexes (POP5/RPP30 and RPP21/RPP29). Archaeal POP5/RPP30 reconstituted with bacterial and organellar RNase P RNAs. While POP5/RPP30 is solely responsible for enhancing the cleavage rate of precursor tRNA by RNase P RNAs (by 60fold), RPP21/RPP29 contributes to increased substrate affinity (by 16-fold)
oligomer
-
the archaeal holoenzyme is associated with 1 RNase P RNA and at least 4 RNase P proteins (POP5, RPP30, RPP21 and RPP29). Archaeal RNase P proteins function as two binary RNase P protein complexes (POP5/RPP30 and RPP21/RPP29). Archaeal POP5/RPP30 reconstituted with bacterial and organellar RNase P RNAs. While POP5/RPP30 is solely responsible for enhancing the cleavage rate of precursor tRNA by RNase P RNAs (by 60fold), RPP21/RPP29 contributes to increased substrate affinity (by 16fold)
oligomer
-
the RNA-binding protein L7Ae (UniProt: Q8U160) is a subunit of the archaeal RNase P ribonucleoprotein complex. The L7Ae protein binds to two kink-turns in the Pyrococcus furiosus RNase P RNA
monomer
-
Rpp25 in solution
additional information
-
-
additional information
-
active holoenzymes can be reconstituted from the Thermotoga aquaticus and the Thermotoga maritima RNAs and the protein component of RNase P from Escherichia coli
additional information
-
RNA and protein subunits from one species can complement subunits from the other species in reconstitution experiments
additional information
-
autoantigenic properties of the protein subunits Rpp38 and Rpp30 of catalytically active complexes of human ribonuclease P
additional information
-
the protein component both alters the conformation of the RNA component and enhances the substrate affinity and specificity
additional information
-
enzyme folding and function are dependent on divalent metal cations, clustered interactions, e.g. with the helix P4 of the enzymes' RNA part, secondary structure of the RNA moiety, overview
additional information
-
enzyme is a ribonucleoprotein consisting of multiple protein components and a single RNA species
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 smaller protein subunit
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
-
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, secondary structure of the enzyme RNA subunit
additional information
-
enzyme secondary structure, domain organization and tertiary structure, modeling, overview
additional information
-
modeling of RNase P holoenzyme assembly, both the mitochondrial and nuclear enzyme complexes are composed of at least 10 protein subunits and 1 RNA subunit H1, overview
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
O59543
protein Ph1877p is one of the essential protein components of the ribozyme and forms a TIM barrel structure consisting of 10 alpha-helices and 7 beta-strands, the protein shows a cluster of positively charged amino acid residues on the molecule surface
additional information
-
protein subunit structure, the enzyme folds as an alpha-beta sandwich and has the overall topology of alpha(beta)3alphabetaalpha, 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
-
ribozyme structure
additional information
-
subunit composition for RNase P: 1 RNA subunit RPM1 plus at least 1 protein subunit Rpm2p for the mitochondrial ribozyme, 9 protein components for the nuclear enzyme form, namely Pop1p, Pop3p-Pop8p, Rpp1p, and Rpr2p, secondary structure of nuclear enzyme RNA, subunit composition for RNase MRP: 1 RNA subunit NME1 plus 9 protein components for the nuclear enzyme form, namely Pop1p, Pop3p-Pop7p, Pop, Rpp1p, and SNM1, overview, Pop7p is also known as Rpp2p
additional information
-
subunit composition, 1 essential RNA subunit
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
-
subunit composition, at least 4 protein subunits namely MTH11, MTH687, MTH688, and MTH1618
additional information
-
subunit composition, secondary structure of the enzyme RNA moiety
additional information
-
subunit interactions, subunit composition for RNase P: 1 RNA subunit RPM1 plus at least 1 protein subunit Rpm2p for the mitochondrial ribozyme, 9 protein components for the nuclear enzyme form, namely Pop1p, Pop3p-Pop8p, Rpp1p, and Rpr2p, secondary structure of nuclear enzyme RNA, subunit composition for RNase MRP: 1 RNA subunit NME1 plus 9 protein components for the nuclear enzyme form, namely Pop1p, Pop3p-Pop7p, Pop, Rpp1p, and SNM1, overview, Pop7p is also known as Rpp2p, structure-function relationship of the RNA subunit
additional information
-
the mitochondrial enzyme contains a single RNa subunit and a single protein subunit
additional information
-
the mitochondrial enzyme contains an RNA subunit and 7 protein subunits of 16-55 kDa
additional information
-
m1 RNA, the catalytic RNA subunit of RNase P is present in two main conformational states, one being characteristic of free RNase P and one of an RNase P-tRNA complex. The C5 protein subunit does not induce the major structural changes
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
-
protein stabilizes the global structure of RNase P RNA and influences holoenzyme dimer formation. 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
-
the enzyme contains an extremely large RNase P RNA subunit, about 1100 nt long
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
-
Nuclear RNase P contains one RNA subunit, RPR1 RNA, and nine protein subunits: Pop1p, Pop3p, Pop4p, Pop5p, Pop6p, Pop7p, Pop8p, Rpp1p, and Rpr2p
additional information
-
RNase P contains an essential RNase P RNA and RNase P protein
additional information
-
RNase P has nine essential protein components (Pop1, Pop3, Pop4, Pop5, Pop6, Pop7, Pop8, Rpp1 and Rpr2)
additional information
-
archaeal RNase P comprises a catalytic RNase P RNA, RPR, and at least four protein cofactors, RPPs, which function as two binary complexes, POP5/RPP30 and RPP21/RPP29
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
-
RNase P RNA solution structure determination using small angle X-ray scattering and selective 29-hydroxyl acylation analyzed by primer extension, SHAPE, analysis, generation of all-atom RNA models, overview
additional information
-
the subunits DRpp29 and RNase P form the holoenzyme RNase P, DRpp29 binds specifically to the RNase P RNA subunit, interaction analysis, overview. An eukaryotic specific, lysine- and arginine-rich region facilitates the interaction between the two subunits. Modeling and prediction of potential RNA binding residues in DRpp29, overview
additional information
-
two aspartates are essential for the activity of PRORP1
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
additional information
-
structure homology modelling of the enzyme's PRORP domain with bound pre-tRNACys from Escherichia coli, overview
additional information
-
the enzyme consists of a catalytic RNA component and nine essential proteins, RNA-protein UV crosslinking studies for structure analysis, comparison to yeast RNase MRP, overview. 3D Mapping of RNA-protein interactions
additional information
-
the enzyme is a ribonlucleoprotein, the RNAsubunit, termed P RNA, contains the active site, whereas the smaller protein subunit, i.e. C5 protein, is required for optimal molecular recognition and catalysis in vitro and is essential in vivo
additional information
-
the enzyme is a ribonucleoprotein consisting of one protein and one RNA subunit, referred to as C5 and RNase P RNA, respectively. The RNase P RNA is composed of domains that have different functions
additional information
-
the enzyme is composed of RNA and five proteins (UniProtIDs: O59425, O59150, O59543, and O59248), the proteins assists the RNA part in attaining a functionally active conformation via a distinct mode of binding
additional information
-
the essential enzyme consists of the C5 protein and the catalytic M1 RNA subunits
additional information
Q9X1H4
wild-type and mutant enzyme structure-function analysis, overview
additional information
-
the subunits DRpp29 and RNase P form the holoenzyme RNase P, DRpp29 binds specifically to the RNase P RNA subunit, interaction analysis, overview. An eukaryotic specific, lysine- and arginine-rich region facilitates the interaction between the two subunits. Modeling and prediction of potential RNA binding residues in DRpp29, overview
-
additional information
Saccharomyces cerevisiae YSW1
-
the enzyme consists of a catalytic RNA component and nine essential proteins, RNA-protein UV crosslinking studies for structure analysis, comparison to yeast RNase MRP, overview. 3D Mapping of RNA-protein interactions
-
additional information
Escherichia coli MG1693
-
the essential enzyme consists of the C5 protein and the catalytic M1 RNA subunits
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ribonucleoprotein
-
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
no ribonucleoprotein
Q66GI4
-
ribonucleoprotein
-
cleaves mitochondrial precursor tRNAHis resulting in an 8-bp acceptor stem
ribonucleoprotein
-
the enzyme requires an RNA as well as a protein subunit for its in vivo activity
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
-
bacterial RNase Ps consist of one RNA and one protein
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)
ribonucleoprotein
-
-
ribonucleoprotein
-
requires a RNA component
ribonucleoprotein
-
the RNA subunit is approximately 400 nucleotides long and makes a precise endonucleolytic cleavage at the mature 5'-terminus of tRNA
ribonucleoprotein
-
-
ribonucleoprotein
-
RNA structural analysis, the enzyme requires an RNA as well as a protein subunit for its in vivo activity
ribonucleoprotein
-
enzyme is a ribonucleoprotein with a large protein part and 1 RNA subunit
ribonucleoprotein
-
the enzyme requires an RNA as well as a protein subunit for its in vivo activity
ribonucleoprotein
-
the M1 RNA component is essential for the function of the enzyme
ribonucleoprotein
-
the catalytic activity resides in the RNA component, the protein cofactor affects the rate of the cleavage reaction
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
-
regions required for the interaction of M1 RNA with C5 protein are localized primarily between nucleotide 82 to 96 and 170 to 270 of M1 RNA
ribonucleoprotein
-
type A enzyme is a ribonucleoprotein and contains a single protein subunit
ribonucleoprotein
-
composed of a catalytic RNA component and an associated protein moiety
ribonucleoprotein
-
the enzyme is a ribonlucleoprotein, the RNAsubunit, termed P RNA, contains the active site, whereas the smaller protein subunit is required for optimal molecular recognition and catalysis in vitro and is essential in vivo
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 a ribonucleoprotein consisting of one protein and one RNA subunit, referred to as C5 and RNase P RNA, respectively
ribonucleoprotein
-
the essential enzyme consists of the C5 protein and the catalytic M1 RNA subunits
ribonucleoprotein
-
-
ribonucleoprotein
-
requires a RNA component
ribonucleoprotein
-
enzyme is a ribonucleoprotein with a large protein part and 1 RNA subunit
ribonucleoprotein
-
most eukaryal nuclear RNase Ps are RNP based, which contain one RNA and at least nine proteins
ribonucleoprotein
-
-
ribonucleoprotein
-
the RNase P RNA lacks essential secondary structures required for the recognition of pre-tRNA and as a result is not catalytically active in vitro
ribonucleoprotein
-
RNase P RNA is catalytically active in the absence of any protein in the appropriate ionic conditions
ribonucleoprotein
-
-
ribonucleoprotein
-
-
no ribonucleoprotein
-
proteinaceous RNase P and chloroplast and mitochondrial enzymes, overview
ribonucleoprotein
-
bacterial-like RNase P and chloroplast and mitochondrial enzymes, overview
ribonucleoprotein
-
the enzyme requires an RNA as well as a protein subunit for its in vivo activity
ribonucleoprotein
-
-
ribonucleoprotein
-
the enzyme is composed of RNA and five proteins (UniProtIDs: O59425, O59150, O59543, and O59248)
ribonucleoprotein
-
ribonucleoprotein complex. RNA subunit is required for activity
ribonucleoprotein
-
contains a highly structured RNA of 369 nucleotides
ribonucleoprotein
-
secondary structure of nuclear RNase P RNA
ribonucleoprotein
-
9S RNA is the RNA component of yeast mitochondrial RNase P
ribonucleoprotein
-
enzyme is a ribonucleoprotein with a large protein part and 1 RNA subunit
ribonucleoprotein
-
most eukaryal nuclear RNase Ps are RNP based, which contain one RNA and at least nine proteins
ribonucleoprotein
-
the enzyme consists of a catalytic RNA component and nine essential proteins
ribonucleoprotein
Saccharomyces cerevisiae SCWY10
-
-
-
ribonucleoprotein
Saccharomyces cerevisiae YSW1
-
the enzyme consists of a catalytic RNA component and nine essential proteins
-
ribonucleoprotein
-
the active site resides within the RNA moiety. The protein has a role in electrostatic shielding and aids in an essential conformational change, the enzyme requires an RNA as well as a protein subunit for its in vivo activity
ribonucleoprotein
-
-
ribonucleoprotein
-
requires a RNA component
ribonucleoprotein
-
-
no ribonucleoprotein
-
-
ribonucleoprotein
-
-
ribonucleoprotein
-
RNA component is not observed to be catalytic by itself
ribonucleoprotein
Q9X1H4
-
ribonucleoprotein
-
bacterial RNase Ps consist of one RNA and one protein
ribonucleoprotein
-
-
no ribonucleoprotein
-
-
no ribonucleoprotein
-
PRORP1 and 2
ribonucleoprotein
-
-
ribonucleoprotein
Escherichia coli MG1693
-
the essential enzyme consists of the C5 protein and the catalytic M1 RNA subunits
-
additional information
-
not a ribonucleoprotein, but a protein enzyme
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis of PRORP enzyme in complex with tRNA
-
hanging drop vapor diffusion method, crystal structure is determined at 1.7 A resolution using X-ray diffraction methods, crystals formed in space group P2(1)2(1)2(1)
-
crystal structure
-
crystallization of the S domain of the RNA subunit, X-ray diffraction structure determination and analysis at 3.15 A resolution, structure modeling
-
crystallographic structure of the S-domain of the enzyme RNA subunit
-
full-length RNase P RNA of type B, to 3.3 A resolution
-
the P7DELTA RNA which is comprised of the independently folding catalytic domain of the RNase P RNA is crystallized by vapour diffusion method with 50 mM Na-cacodylate at pH 6.5, 100 mM KCL, 0.7-1.0 mM spermidine tetrachloride, and 21-23% 1,6-hexanediol
-
vapor diffusion method, X-ray crystal structure of ribonuclease RNA solved to 3.3 A resolution
-
crystal structure analysis of PRORP enzyme in complex with tRNA
-
hanging drop vapor diffusion, structure of Pfu Pop5, an archaeal RNase P protein. Crystals of Pfu Pop5 belong to the P4(1)2(1)2 space group and have five monomers in the asymmetric unit
Q8U151
10 mg/ml purified recombinant selenomethionine labeled protein subunit Ph1877p, vapour diffusion against 22.5% PEG 6000 and 0.1 M HEPES, pH 7.5, hanging drop method, crystals are suspended on a loop in a thin liquid film of stabilizing solution and frozen directly for X-ray diffraction structure determination and analysis at 1.8 A resolution
O59543
hanging drop vapor diffusion, structure of protein Ph1481p (subunit of RNase P) in complex with protein Ph1877p (subunit of RNase P), 2.0 A resolution
-
PhoRpp21 and PhoRpp29, hanging drop vapour diffusion method. using 50 mM Tris-HCl (pH 7.5) containing 50 mM sodium chloride, 200 mM potassium nitrate, and 20% w/v PEG 3350
O59425
structure of mutant ribunuclease P protein Ph1771p, which lacks the N-terminal 31 amino acids and contains a C93S mutation is determined at 2.0 A resolution, sitting drop vapor diffusion method
-
vapor diffusion against 0.2 M triammonium citrate, pH 7.0, 20% v/v polyethylene glycol 3350, 10 mM ZnCl2 and 10% v/v ethanol. Stucture of a ribonuclease P protein Ph1601p determined at 1.6 A resolution with the aid of anomalous signals from selenomethionines and zinc ion
-
complex including a circularly permuted 46-nucleotide-long P3 domain of the RNA component of ribonuclease MRP and selenomethionine derivatives of the shared ribonuclease P/MRP protein components Pop6 and Pop7, using the sitting-drop vapour-diffusion method. The crystals belong to space group P4222 with unit-cell parameters a = b = 127.2, c = 76.8 A , alpha = beta = gamma = 90 and diffract to 3.25 A resolution. The terminal part of the proximal helical stem of the P3 domain is not involved in interactions with Pop6-Pop7
-
3 possible RNA-binding motifs, including a putative single-stranded RNA-binding cleft formed by an alpha-helix and a four-stranded beta-sheet, derived from crystal structure and NMR study
-
crystal structure analysis of RNase P enzyme in complex with tRNA, PDB ID 3Q1R
-
crystal structure of the RNA component of ribonuclease P at 3.85 A resolution
-
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
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
67
-
Tm-value of the protein component
134454
999
-
thermostable
678540
additional information
-
mutations which affect either the protein or RNA component of RNase P can confer thermal sensitivity on the enzyme both in vivo and in vitro. The protein component of RNase P from ts241 and the RNA component of RNase P from ts709, respectively, account for the thermal sensitivity of the RNase P from the two strains
134429
additional information
P25814
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
664073
additional information
P62426 and P60780 and P60781 and P60832 and P62378
ribosomal protein L7Ae increases the thermostability of the RNase P holoenzyme, the secondary structure is not different from that of the wild type enzyme
728660
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Ca2+, Sr2+ and Mg2+ maintain the structure of the enzyme in solution
-
spermidine and spermine maintain the structure of the enzyme in solution
-
complete inactivation by proteases subtilisin BPN', proteinase K, and pronase
-
resistant to rigorous treatments with nucleases
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, 50 mM Tris /HCl pH 7.5, 100 mM NH4Cl, 5 mm MgCl2, 2.5 mM EGTA, and 0.5 U RNasin, few weeks, the enzyme activity remains stable
-
4C, 10 mM Tris-HCl buffer, pH 7.4, 100 mM NaCl, 50 mM KCl, 2 mM DTT, 0.1 mM Na EDTA and 0.1 mM PMSF, several weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain Rosetta (DE3)pLysS by nickel affinity chromatography
L0N807
to homogeneity
-
P protein purified by ion exchange chromatography under denaturing conditions
-
partially purified
-
protein component
-
recombinant untagged and His-tagged enzymes
-
RNA moiety
-
RNA subunit, partial
-
by Ni-NTA affinity chromatography
-
Ni-NTA column chromatography
-
partially purified by ion-exchange chromatography
-
protein moiety. Reconstitution of the holoenzyme when mixed with M1 RNA
-
recombinant untagged and His-tagged enzymes
-
RNA moiety
-
partial
-
Q sepharose column chromatography
-
affinity purification
-
DEAE-Sepharose column chromatography and Sephacryl S-100 gel filtration
-
mitochondrial enzyme, and RNase P partially
-
MRPP1, affinity purified
-
partial
-
partial purification into protein and RNA subunit. Reconstitution of homologous enzyme complex and heterologous enzyme complexes with subunits from the Escherichia coli enzyme
-
partially purified by DEAE Sepharose column chromatography
-
phosphocellulose column chromatography
-
recombinant His-tagged subunits Rpp14, Rpp20, Rpp21, Rpp25, Rpp29, Rpp30, Rpp38, Rpp40, and hPop5 from Escherichia coli as soluble and refolded proteins
-
recombinant protein and RNA subunits H1, Rpp21, and Rpp29 from Escherichia coli
-
recombinant protein subunit Rpp25, and native wild-type enzyme from HeLa cells
-
partial. The RNase P RNA lacks essential secondary structures required for the recognition of pre-tRNA and as a result is not catalytically active in vitro
-
partially, 2400fold
-
recombinant enzyme from Escherichia coli strain BL21(DE3) by cation exchange and metal chelating affinity chromatography
Q00XA5
HiTrap column chromatography and C4 reversed-phase high performance liquid chromatography
Q8U0H6
purified to homogeneity by using cation-exchange and reversed-phase chromatography
-
RPP21 and RPP29. RPP29 eluted and ultrafiltrated
-
recombinant wild-type and mutant protein subunits from Escherichia coli
O59543
SP-Sepharose column chromatography
O59425
affinity purified
-
copurified with nuclear RNAs by aptamer-streptavidin affinity chromatography and TAP column chromatography
-
nuclear enzyme
-
RNase P from nucleus
-
tandem affinity chromatography
-
tandem affinity purification tag chromatography, calmodulin affinity resin chromatography, and DEAE Sepharose column chromatography
-
native nuclear enzyme partially purified from leaves employing anion exchange chromatography, and from floral buds employing two different steps of anion exchange chromatography, ammonium sulfate fractionation, and gel filtration, purification of recombinant His6-tagged proteins StPop5 and StRpp25 from Escherichia coli strain BL21(DE3)
-
partially from 800-900fold over the chloroplast lysate
-
RNase P from Sulfolubus solfataricus is purified 800fold by Trisacryl-DEAE, and Sepharose CL-6B chromatographies and Cs2S04 buoyant density centrifugation
-
recombinant enzyme
-
recombinant GST-tagged wild-type and mutant proteins and RNA from Escherichia coli strain BL21(DE3)pLysS
Q9X1H4
recombinant protein subunit from Escherichia coli, to homogeneity
-
recombinant C-terminally His6-tagged PRORP1 from Escherichia coli by nickel affinity chromatography, recombinant C-terminally His6-tagged and N-terminally GST-tagged PRORP2 from Escherichia coli by nickel and glutathione affinity chromatography, and proteolytical cleavage of the GST-tag, both proteins ar further purified by gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene At2g47290, DNA and amino acid sequence determination and analysis, AtPop1 mRNA is present in multiple splicing isoforms, possibly encoding several distinct proteins, splicing patterns of AtPop1 mRNAs, overview. Recombinant expression in Escherichia coli strain Rosetta (DE3)pLysS
L0N807
PRORP1-PRORP3, phylogenetic analysis, overview
-
expression in Escherichia coli. the protein is homologous to the human RNase P protein Rpp29, yeast RNase P protein Pop4, and an archaeal RNase P protein from Methanobacter thermoautotrophicus
-
gene for the RNA subunit
-
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
-
gene for the protein moiety
-
gene for the protein moiety; overproduced in Escherichia coli
-
gene for the RNA component
-
N-terminal His-tagged RNase P protein overexpressed
-
gene for the RNA subunit
-
subunits DRpp29 and RNase P
-
cloning of mutant enzyme in amphotropic packaging PA317 cells, heterologous expression of wild-type and mutant enzymes in human H9 cells
-
Escherichia coli transformed with a plasmid expressing RNase P RNA
-
expressed in Escherichia coli strain JM109
-
expression of wild-type and mutant enzymes in Escherichia coli
-
expression of wild-type enzyme by in vitro transcription, expression of His-tagged enzyme
-
gene for the protein moiety
-
N-terminal His-tagged RNase P protein overexpressed
-
pET-15b-derived plasmid endcoding the C5 protein expressed in Escherichia coli BL21(DE3). Into pUC19 vector and transformed into Escherichia coli strain JM109
-
plasmids carrying the M1GS constructs delivered to murine cytomegalovirus-infected mice by a hydrodynamic transfection procedure
-
protein overexpressed in Escherichia coli with an N-terminal hexahistidyl tag, RNA subunit produced by run-off in vitro T7 transcription from plasmid pDW98 linearized with BsaAI
-
the RNase P ribozyme subunit is expressed in Escherichia coli BL21(DE3) cells
-
gene for the RNA subunit
-
cDNAs of full-length Rpp20 and Rpp25 cloned into pCR4-TOPO. Full-length Rpp25 (encompassing residues 1-199) subcloned with an N-terminal hexahistidine tag into a pPROEX-HTb expression vector using Nco1/Not1 restriction sites. Full-length Rpp20 (residues 1-140) subcloned into a pET-30 expression vector. The pET-30 vector modified to bear a TEV cleavage site to remove the N-terminal hexahistidine tag. Mutant Rpp20(35-140) amplified from pET-30 Rpp20 to introduce 5' Asc1 and 3' Not1 sites and then ligated into a modified version of pET-15b vector with an Asc1 site inserted directly after the his tag. Fragments Rpp20, mutant Rpp20(16-140), mutant Rpp25(25-170) and co-expressed Rpp20/Rpp25 (in which Rpp20 bears the his tag) subcloned in pETDuet-1 vector with an N-terminal hexahistidine tag. Mutant Rpp25(25-170) also subcloned in a pCDFDuet-1 vector also with an N-terminal hexahistidine tag. Rpp25, Rpp20 (from pET-30 vector) and mutant Rpp20(35-140) expressed in Escherichia coli strain BL21(DE3)pLysS. All the other proteins subcloned into pETDuet-1 or pCDFDuet-1 vectors expressed in Escherichia coli KRX strain
-
chromosomal localization of genes encoding the RNase P subunits
-
expression of His-tagged protein subunits Rpp29, Rpp21, and RNA subunit H1 in Escherichia coli BL21(DE3)
-
expression of His-tagged subunits Rpp14, Rpp20, Rpp21, Rpp25, Rpp29, Rpp30, Rpp38, Rpp40, and hPop5 in Escherichia coli
-
expression of wild-type and mutant external guide sequences in brief, amphotropic PA317 cells
-
expression of wild-type enzyme and protein subunit Rpp25 in Escherichia coli
-
tagged overexpression of MRPP1, MRPP2 and MRPP3 in human cells
-
DNA and amino acid sequence determination and analysis, in vitro transcription, and overexpression in Escherichia coli strain BL21(DE3)
Q00XA5
expressed in Escherichia coli, TOPO-TA cloning vector, in vitro transcription
-
gene for the RNA subunit
-
expressed in Escherichia coli Rosetta BL21(DE3) cells
Q8U0H6
overexpression in Escherichia coli BL21(DE3) Rosetta cells
-
RPP21 and RPP29. RPP29/pET-33b plasmid transformed into Escherichia coli BL21(DE3) Rosetta cells
-
overexpression of native and selenomethionine-containing wild-type protein subunit Ph1877p, and mutant protein subunits Ph1788p in Escherichia coli
O59543
expression of His-tagged enzyme, co-expression of C-terminally TAP-tagged RNaseP with C-terminally TAP-tagged yeast RNase MRP
-
full-length Pop6 and Pop7 coexpressed in Escherichia coli. Selenomethionine derivative of the Pop6-Pop7 heterodimer obtained using Escherichia coli strain BL21
-
DNA and amino acid sequence determination and analysis of two cDNAs encoding two putative protein subunits of potato ribonuclease P, StPop5 and StRpp25, subcloning in Escherichia coli strain M15, recombinant overexpression as His6-tagged proteins in Escherichia coli strain BL21(DE3)
-
overexpression in Escherichia coli
-
DNA sequence coding for mutants M1-C1 and M1-C2 cloned into vector pU6, which contains a GFP expression cassette, and placed under the control of the small nuclear U6 RNA promoter. DNA sequence for ribozyme M1-thymidine kinase, which is derived from V57 and targets the herpes simplex virus 1 thymidine kinase mRNA, also cloned into vector pU6. Transformed into Salmonella typhimurium aroA strain SL7207
synthetic construct
-
genes rnpA and rnpB, recombinant expression of GST-tagged wild-type and mutant proteins and RNA in Escherichia coli strain BL21(DE3)pLysS
Q9X1H4
overexpression of the protein subunit in Escherichia coli
-
genes PRORP1 and PRORP2, recombinant expression of C-terminally His6-tagged PRORP1 and of C-terminally His6-tagged and N-terminally GST-tagged PRORP2 in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
RNase P RNA expression decreases during the stringent response induced by amino acid starvation/cis-acting sequences in the RNase P RNA promoter
-
when plasmids carrying the M1GS constructs are delivered to murine cytomegalovirus-infected mice by a hydrodynamic transfection procedure, the M1GS RNA is expressed in a substantial amount in the livers and spleens of the animals
-
down-regulation of a single RNase P protein in cultured human cells results in a concomitant decrease of up to four other RNase P proteins (but not the RNase P RNA), likely due to transcriptional repression
-
RNase P-external guide sequence and short hairpin RNAi technologies have about equal levels of inhibition of RNase P protein subunits
-
Salmonella RNase P-based ribozyme sequence delivered in specific human cells, leads to substantial ribozyme expression. The M1GS RNAs appears to be exclusively expressed in the nuclei
synthetic construct
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C344A
-
site-directed mutagenesis, the mutant shows a 19% reduced zinc level compared to the wild-type enzyme
C347A
-
site-directed mutagenesis, the mutant shows a 29% reduced zinc level compared to the wild-type enzyme
C565A
-
site-directed mutagenesis, the mutant shows a 75% reduced zinc level compared to the wild-type enzyme
C56A
-
site-directed mutagenesis, the mutant shows no enzyme activity
C56G
-
site-directed mutagenesis, the mutant shows no enzyme activity
C57A
-
site-directed mutagenesis, the mutant shows 90% of wild-type enzyme activity
C57C
-
site-directed mutagenesis, the mutant shows 10% of wild-type enzyme activity
D474A/D475A
-
site-directed mutagenesis, the mutant shows 3,3% reduction of the zinc level compared to the wild-type enzyme
G18A
-
site-directed mutagenesis, the mutant shows 15% of wild-type enzyme activity
G18C
-
site-directed mutagenesis, the mutant shows 10% of wild-type enzyme activity
G19A
-
site-directed mutagenesis, the mutant shows 85% of wild-type enzyme activity
G19C
-
site-directed mutagenesis, the mutant shows 90% of wild-type enzyme activity
H548A
-
site-directed mutagenesis, the mutant shows a 60% reduced zinc level compared to the wild-type enzyme
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
F16C
-
increases