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Information on EC 3.1.26.5 - ribonuclease P and Organism(s) Homo sapiens
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3.1.26.5 ribonuclease PSpecify your search results
Word Map
- 3.1.26.5
- ribonucleoproteins
- pre-trnas
-
endoribonuclease
-
endonucleolytic
- eculizumab
- aminoacylation
-
rna-based
-
stem-loops
-
phosphodiester
-
nucleolar
-
nocturnal
-
eubacterial
-
paroxysmal
-
gene-targeting
-
anticodon
-
base-pairing
-
rna-protein
- sars-cov-2
- c5a
- horikoshii
- hemoglobinuria
-
trna-like
- pyrococcus
-
swab
-
3'-terminal
-
5\'-leader
- riboswitches
- trnatyr
-
2'-hydroxyls
- trnahis
- trailer
-
cloverleaf
-
rna-rna
-
self-splicing
-
protein-rna
- tmrna
-
micrococcal
-
self-cleaving
-
t-loops
-
p-mediated
-
complement-mediated
- ncrnas
-
pseudoknots
-
watson-crick
-
eukaryal
- oligoribonucleotides
- analysis
- pharmacology
-
snornps
- synthesis
- medicine
- biotechnology
-
trnase
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
Synonyms
rnase p, rnase p rna, rnase mrp, ribonuclease p, m1 rna, c5 protein, rnase p protein, rnase p holoenzyme, rpp30, protein c5, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
hPOP1
-
-
-
-
hPOP4
-
-
-
-
hPOP7
-
-
-
-
nuclease, ribo-, P
-
-
-
-
Protein C5
-
-
-
-
ribonuclease P
RNA processing protein POP1
-
-
-
-
RNA processing protein POP5
-
-
-
-
RNA processing protein POP6
-
-
-
-
RNA processing protein POP7
-
-
-
-
RNA processing protein POP8
-
-
-
-
RNase P
RNase P protein
-
-
-
-
RNaseP protein
-
-
-
-
RNaseP protein p20
-
-
-
-
RNaseP protein p30
-
-
-
-
RNaseP protein p38
-
-
-
-
RNaseP protein p40
-
-
-
-
ribonuclease P
-
-
-
-
RNase P
-
-
-
-
RNase P
-
-
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
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, 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
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, the RNA subunit is essential for catalytic activity, divalent metal ion-dependent in-line SN2 displacement mechanism
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, 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
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, tRNA precursor substrate recognition and cleavage mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
CAS REGISTRY NUMBER
COMMENTARY
71427-00-4
not distinguished from EC 3.1.26.7
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pre-rRNA + H2O
mature rRNA
-
enzyme RNase MRP plays an important role in pre-rRNA processing
-
-
?
pre-tRNA + H2O
?
-
in mitochondria, RNase P function has been taken over by an unrelated, protein-only enzyme activity
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-terminal oligonucleotide
-
enzyme is responsible for removing the 5'-leader segment of precursor tRNA during maturation
-
-
?
tRNATyr precursor + H2O
mature tRNATyr + 5'-oligonucleotide
-
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
-
?
tRNATyrUAG precursor + H2O
?
-
RNase P cleavage of this substrate generates a 5' matured tRNA with a 7 base pair amino acceptor stem
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
autoantigenic properties of the protein subunits Rpp38 and Rpp30 of catalytically active complexes of human ribonuclease P
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
involved in biosynthesis of KB cell tRNA
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
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
-
removes 5' extensions from genuine mitochondrial tRNA precursors
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
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
-
cleaves the precursor to E. coli suppressor tRNATyr at the same site as E. coli RNase P
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
E. coli tRNATyr precursor
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
5'-leader sequence tRNA processing, essential enzyme
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide, maturation
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide, maturation, essential
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
essential enzymes in the biogenesis of tRNA, maturation
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
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
-
?
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
?
-
-
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
?
-
-
substrate specificities of enzyme forms RNase P and RNase MRP
-
-
?
additional information
?
-
-
the recombinant holoenzyme and the Rpp20p subunit display ATPase activity
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pre-rRNA + H2O
mature rRNA
-
enzyme RNase MRP plays an important role in pre-rRNA processing
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-terminal oligonucleotide
-
enzyme is responsible for removing the 5'-leader segment of precursor tRNA during maturation
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
autoantigenic properties of the protein subunits Rpp38 and Rpp30 of catalytically active complexes of human ribonuclease P
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
involved in biosynthesis of KB cell tRNA
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
5'-leader sequence tRNA processing, essential enzyme
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide, maturation
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide, maturation, essential
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
essential enzymes in the biogenesis of tRNA, maturation
-
-
?
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
?
-
-
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
K+
Mg2+
Mn2+
Na+
NH4+
additional information
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+
-
dependent on, the optimum is at 5 mM MgCl2, when reactions are carried out at pH 7.5 and 37°C
Mg2+
-
enzymatic activity depends on the presence of divalent metal ions such as Mg2+
Mg2+
-
mitochondrial RNase P requires divalent metal ions, preferably Mg2+, for cleavage
NH4+
-
monovalent cation required: Na+, K+ or NH4+. Optimal NH4+ concentration is 200 mM
NH4+
-
dependent on, the optimum is at 70 mM NH4Cl, when reactions are carried out at pH 7.5 and 37°C
additional information
-
divalent metal ions are absolutely required, reduced activity with Ca2+
additional information
-
divalent metal ions are important cofactors for the reaction
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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%)
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.074
neomycin B
Homo sapiens
-
in 50 mM Tris /HCl pH 7.5, 100 mM NH4Cl, 5 mM MgCl2, 2.5 mM EGTA and 0.5 U Rnasin
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.6 - 4.7
5.5
6.9
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
134413, 134415, 134421, 134435, 134443, 134461, 134462, 654201, 656107, 656352, 656772, 657340, 657341, 691597, 691665, 691666, 692220, 692711, 694828, 708512, 709859, 710127, 710148, 710543, 710544, 716376, 716391, 730931, 730933
-
-
human RNase P consists of a catalytic RNA moiety and about 10 protein subunits; POP1 (Q99575), POP4 (O95707), POP5 (Q969H6), POP7 (O75817), RPP14 (O95059), RPP21 (Q9H633), RPP25 (Q9BUL9), RPP30 (P78346), RPP38 (P78345) and RPP40 (O75818)
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
all putative components of the enzyme are encoded by the nucleus
-
the RNA subunits of the mitochondrial and nuclear enzymes are identical
-
the RNA subunits of the mitochondrial and nuclear enzymes are identical
additional information
-
eukaryotic cells may contain multiple RNase P activities, a nucear type as well as enzyme species in mitochondria and chloroplasts
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
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
-
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
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
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
-
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 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
-
nuclear RNase P is required for transcription and processing of tRNA
physiological function
-
the enzyme catalyzes the maturation of the 5' end of precursor-tRNAs
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MRPP3_HUMAN
583
0
67315
Swiss-Prot
Mitochondrion (Reliability: 5)
RPP38_HUMAN
283
0
31834
Swiss-Prot
other Location (Reliability: 1)
RPP40_HUMAN
363
0
41834
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
105000
-
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
115000
-
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
13200
-
2 * 16000, full-length Rpp20, gel filtration. 2 * 14100, Rpp20(16-140), gel filtration. 2 * 13200, HisRpp20(35-140), gel filtration
14000
-
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
14100
-
2 * 16000, full-length Rpp20, gel filtration. 2 * 14100, Rpp20(16-140), gel filtration. 2 * 13200, HisRpp20(35-140), gel filtration
16000
-
2 * 16000, full-length Rpp20, gel filtration. 2 * 14100, Rpp20(16-140), gel filtration. 2 * 13200, HisRpp20(35-140), gel filtration
20000
-
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
21000
-
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
25000
-
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
29000
-
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
30000
-
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
38000
-
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
40000
-
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
-
2 * 16000, full-length Rpp20, gel filtration. 2 * 14100, Rpp20(16-140), gel filtration. 2 * 13200, HisRpp20(35-140), gel filtration
oligomer
additional information
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
additional information
-
autoantigenic properties of the protein subunits Rpp38 and Rpp30 of catalytically active complexes of human ribonuclease P
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
the RNase P complex for 5'-end cleavage comprises the methyltransferase domain-containing protein tRNA methyltransferase 10C, mitochondrial RNase P subunit (TRMT10C/MRPP1), short-chain oxidoreductase hydroxysteroid 17'-dehydrogenase 10 (HSD17B10/MRPP2), and metallonuclease KIAA0391/MRPP3
additional information
-
the RNase P complex for 5'-end cleavage comprises the methyltransferase domain-containing protein tRNA methyltransferase 10C, mitochondrial RNase P subunit (TRMT10C/MRPP1), short-chain oxidoreductase hydroxysteroid 17'-dehydrogenase 10 (HSD17B10/MRPP2), and metallonuclease KIAA0391/MRPP3
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ribonucleoprotein
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 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
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial purification into protein and RNA subunit. Reconstitution of homologous enzyme complex and heterologous enzyme complexes with subunits from the Escherichia coli enzyme
-
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
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
ORGANISM
UNIPROT
LITERATURE
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
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of a functional mini-enzyme from protein subunits Rpp21 and Rpp29 with the RNA subunit H1, all 3 coponents are essential for reconstitution
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
construction of external guide sequences (EGSs) from a variant to target the mRNA encoding herpes simplex virus 1 (HSV-1) major transcription regulator ICP4, which is essential for the expression of viral early and late genes and viral growth. The EGS variant induces human RNase P cleavage of ICP4 mRNA sequence 60times better than the EGS generated from a natural pre-tRNA. A decrease of about 97% and 75% in the level of ICP4 gene expression and an inhibition of about 7,000- and 500-fold in viral growth are observed in HSV infected cells expressing the variant and the pre-tRNA-derived EGS, respectively. The study shows that engineered external guide sequences (EGSs) can inhibit HSV-1 gene expression and viral growth. The results demonstrate the potential for engineered EGS RNAs to be developed and used as anti-HSV therapeutics
pharmacology
-
specific external guide sequences offer a possibility for specific decrease of gene expression by inhibition of RNase P
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Altman, S.
Ribonuclease P: an enzyme with a catalytic RNA subunit
Adv. Enzymol. Relat. Areas Mol. Biol.
62
1-36
1989
Bos taurus, Escherichia coli, Haloferax volcanii, Homo sapiens
Pace, N.R.; Smith, D.
Ribonuclease P: function and variation
J. Biol. Chem.
265
3587-3590
1990
Bacillus subtilis, Saccharomyces cerevisiae, Homo sapiens, Schizosaccharomyces pombe, Xenopus laevis
Gold, H.A.; Altman, S.
Reconstitution of RNAase P activity using inactive subunits from E. coli and HeLa cells
Cell
44
243-249
1986
Escherichia coli, Homo sapiens
Koski, R.A.; Bothwell, A.L.M.; Altman, S.
Identification of a ribonuclease P-like activity from human KB cells
Cell
9
101-116
1976
Escherichia coli, Homo sapiens
Doersen, C.J.; Guerrier-Takada, C.; Altman, S.; Attardi, G.
Characterization of an RNase P activity from HeLa cell mitochondria. Comparison with the cytosol RNase P activity
J. Biol. Chem.
260
5942-5949
1985
Homo sapiens
Jarrous, N.; Eder, P.S.; Guerrier-Takada, C.; Hoog, C.; Altman,S.
Autoantigenic properties of some protein subunits of catalytically active complexes of human ribonuclease P
RNA
4
407-417
1998
Homo sapiens
Rossmanith, W.; Karwan, R.M.
Characterization of human mitochondrial RNase P: novel aspects in tRNA processing
Biochem. Biophys. Res. Commun.
247
234-241
1998
Homo sapiens
Xiao, S.; Scott, F.; Fierke, C.A.; Engelke, D.R.
Eukaryotic ribonuclease P: a plurality of ribonucleoprotein enzymes
Annu. Rev. Biochem.
71
165-189
2002
Bacillus subtilis, Saccharomyces cerevisiae, Cyanophora paradoxa, Escherichia coli, Homo sapiens, Methanothermobacter thermautotrophicus, Nicotiana tabacum, Spinacia oleracea
Gopalan, V.; Vioque, A.; Altman, S.
RNase P: variations and uses
J. Biol. Chem.
277
6759-6762
2002
Aspergillus nidulans, Bacillus subtilis, Saccharomyces cerevisiae, Cyanophora paradoxa, Escherichia coli, Homo sapiens, Leishmania sp., Mus musculus, Trypanosoma sp.
Xiao, S.; Houser-Scott, F.; Engelke, D.R.
Eukaryotic ribonuclease P: increased complexity to cope with the nuclear pre-tRNA pathway
J. Cell. Physiol.
187
11-20
2001
Bacillus subtilis, Bacteria, Saccharomyces cerevisiae, Cyanophora paradoxa, Homo sapiens, Spinacia oleracea
Mann, H.; Ben-asouli, Y.; Schein, A.; Moussa, S.; Jarrous, N.
Eukaryotic RNase P: role of RNA and protein subunits of a primordial catalytic ribonucleoprotein in RNA-based catalysis
Mol. Cell
12
925-935
2003
Homo sapiens
Jarrous, N.
Human ribonuclease P: subunits, function, and intranuclear localization
RNA
8
1-7
2002
Saccharomyces cerevisiae, Homo sapiens
Guerrier-Takada, C.; Eder, P.S.; Gopalan, V.; Altman, S.
Purification and characterization of Rpp25, an RNA-binding protein subunit of human ribonuclease P
RNA
8
290-295
2002
Homo sapiens
Bassett, T.; Harpur, B.; Poon, H.Y.; Kuo, K.H.; Lee, C.H.
Effective stimulation of growth in MCF-7 human breast cancer cells by inhibition of syntaxin18 by external guide sequence and ribonuclease P
Cancer Lett.
272
167-175
2008
Homo sapiens
Walker, S.C.; Engelke, D.R.
A protein-only RNase P in human mitochondria
Cell
135
412-414
2008
Homo sapiens
Holzmann, J.; Frank, P.; Loeffler, E.; Bennett, K.L.; Gerner, C.; Rossmanith, W.
RNase P without RNA: identification and functional reconstitution of the human mitochondrial tRNA processing enzyme
Cell
135
462-474
2008
Homo sapiens
Vourekas, A.; Vryzaki, E.; Toumpeki, C.; Stamatopoulou, V.; Monastirli, A.; Tsambaos, D.; Drainas, D.
Partial purification and characterization of RNase P from human peripheral lymphocytes
Exp. Dermatol.
18
130-133
2009
Homo sapiens
Kirsebom, L.A.; Trobro, S.
RNase P RNA-mediated cleavage
IUBMB Life
61
189-200
2009
Bacillus subtilis, Chlamydia sp., Homo sapiens, no activity in Nanoarchaeum equitans
Reiner, R.; Krasnov-Yoeli, N.; Dehtiar, Y.; Jarrous, N.
Function and assembly of a chromatin-associated RNase P that is required for efficient transcription by RNA polymerase I
PLoS ONE
3
e4072
2008
Homo sapiens
Lai, L.B.; Vioque, A.; Kirsebom, L.A.; Gopalan, V.
Unexpected diversity of RNase P, an ancient tRNA processing enzyme: challenges and prospects
FEBS Lett.
584
287-296
2010
Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Methanothermobacter thermautotrophicus
Holzmann, J.; Rossmanith, W.
tRNA recognition, processing, and disease: hypotheses around an unorthodox type of RNase P in human mitochondria
Mitochondrion
9
284-288
2009
Homo sapiens
Lundblad, E.W.; Altman, S.
Inhibition of gene expression by RNase P
New Biotechnol.
27
212-221
2010
Synechocystis sp., Escherichia coli, Homo sapiens, Spinacia oleracea, no activity in Nanoarchaeum equitans, Ignicoccus hospitalis
Hands-Taylor, K.L.; Martino, L.; Tata, R.; Babon, J.J.; Bui, T.T.; Drake, A.F.; Beavil, R.L.; Pruijn, G.J.; Brown, P.R.; Conte, M.R.
Heterodimerization of the human RNase P/MRP subunits Rpp20 and Rpp25 is a prerequisite for interaction with the P3 arm of RNase MRP RNA
Nucleic Acids Res.
38
4052-4066
2010
Homo sapiens
Ellis, J.; Brown, J.
The RNase P family
RNA Biol.
6
362-369
2009
Cupriavidus necator, Bacillus subtilis, Saccharomyces cerevisiae, Chlamydia trachomatis, Chlorobium limicola, Escherichia coli, Giardia intestinalis, Homo sapiens, Methanothermobacter thermautotrophicus, Methanocaldococcus jannaschii, Mycoplasmopsis fermentans, Mycoplasma hyopneumoniae, no activity in Aquifex aeolicus, Pyrobaculum aerophilum, Thermomicrobium roseum, Porphyra purpurea, Synechococcus elongatus PCC 6301, Reclinomonas americana
Marvin, M.C.; Engelke, D.R.
RNase P: increased versatility through protein complexity?
RNA Biol.
6
40-42
2009
Saccharomyces cerevisiae, Homo sapiens
Jarrous, N.; Gopalan, V.
Archaeal/eukaryal RNase P: subunits, functions and RNA diversification
Nucleic Acids Res.
38
7885-7894
2010
Saccharomyces cerevisiae, [Candida] glabrata, Escherichia coli, Homo sapiens, Methanothermobacter thermautotrophicus, Mus musculus, Mycoplasmopsis fermentans, Pyrococcus furiosus, Saccharolobus solfataricus
Reiner, R.; Alfiya-Mor, N.; Berrebi-Demma, M.; Wesolowski, D.; Altman, S.; Jarrous, N.
RNA binding properties of conserved protein subunits of human RNase P
Nucleic Acids Res.
39
5704-5714
2011
Homo sapiens
Howard, M.J.; Liu, X.; Lim, W.H.; Klemm, B.P.; Fierke, C.A.; Koutmos, M.; Engelke, D.R.
RNase P enzymes: divergent scaffolds for a conserved biological reaction
RNA Biol.
10
909-914
2013
Bacillus subtilis, Saccharomyces cerevisiae, Homo sapiens, Thermotoga maritima, Trypanosoma brucei, Ostreococcus tauri, Arabidopsis thaliana (Q66GI4), Arabidopsis thaliana
Jiang, X.; Chen, Y.C.; Gong, H.; Trang, P.; Lu, S.; Liu, F.
Ribonuclease P-mediated inhibition of human cytomegalovirus gene expression and replication induced by engineered external guide sequences
RNA Biol.
9
1186-1195
2012
Homo sapiens
Oerum, S.; Roovers, M.; Rambo, R.P.; Kopec, J.; Bailey, H.J.; Fitzpatrick, F.; Newman, J.A.; Newman, W.G.; Amberger, A.; Zschocke, J.; Droogmans, L.; Oppermann, U.; Yue, W.W.
Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes
J. Biol. Chem.
293
12862-12876
2018
Homo sapiens (O15091), Homo sapiens
Liu, J.; Shao, L.; Trang, P.; Yang, Z.; Reeves, M.; Sun, X.; Vu, G.P.; Wang, Y.; Li, H.; Zheng, C.; Lu, S.; Liu, F.
Inhibition of herpes simplex virus 1 gene expression and replication by RNase P-associated external guide sequences
Sci. Rep.
6
27068
2016
Homo sapiens (Q99575 AND O95707 AND Q969H6 AND O75817 AND O95059 AND Q9H633 AND Q9BUL9 AND P78346 AND P78345 AND O75818), Homo sapiens
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