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Information on EC 3.1.26.5 - ribonuclease P and Organism(s) Pyrococcus furiosus and UniProt Accession Q8U151
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3.1.26.5 ribonuclease PSpecify your search results
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- 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: Pyrococcus furiosus
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
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
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-tRNA + H2O
tRNA + 5' leader of tRNA
-
RNase P holoenzymes, reconstituted in vitro
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
cleaves the 5'-leader sequence of precursor tRNAs during their maturation
-
-
?
pre-tRNATyr + H2O
tRNATyr + 5'-oligoribonucleotide
-
pre-tRNATyr from Escherichia coli
-
-
?
precursor tRNA + H2O
?
-
catalyzes the magnesium-dependent 5'-end maturation of tRNAs
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
precursor tRNA + H2O
?
-
catalyzes the magnesium-dependent 5'-end maturation of tRNAs
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
-
optimal 120 mM RNase P RNA + RNase P protein 21 + RNase P protein 29
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
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
physiological function
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
-
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
-
RNase P plays a role in precursor tRNA processing
physiological function
-
the enzyme catalyzes the Mg2+-dependent 5'-maturation of precursor tRNAs
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oligomer
additional information
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 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
additional information
-
RNase P contains an essential RNase P RNA and RNase P protein
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A14V
-
RPP21 mutant, wild-type RPP21 binds to RPP29 3fold tighter than the mutant
C71V
-
the single-Cys substitutions are introduced into a Cys-less Pfu L7Ae template C71V (i.e. RNA-binding protein L7Ae, subunit of archaeal RNase P). The native C71, which is partly buried, is mutated to Val to preserve the native fold and hydrophobic core of the protein. The C71V parental reference is more active than the wild type enzyme
K42C
-
mutation does not affect activity. The single-Cys substitution is introduced into a Cys-less Pfu L7Ae template C71V (i.e. RNA-binding protein L7Ae, subunit of archaeal RNase P). The native C71, which is partly buried, is mutated to Val to preserve the native fold and hydrophobic core of the protein
R46C
-
mutation results in 28% decrease in activity. The single-Cys substitution is introduced into a Cys-less Pfu L7Ae template C71V (i.e. RNA-binding protein L7Ae, subunit of archaeal RNase P). The native C71, which is partly buried, is mutated to Val to preserve the native fold and hydrophobic core of the protein
V95C
-
mutation results in 6% decrease in activity. The single-Cys substitution is introduced into a Cys-less Pfu L7Ae template C71V (i.e. RNA-binding protein L7Ae, subunit of archaeal RNase P). The native C71, which is partly buried, is mutated to Val to preserve the native fold and hydrophobic core of the protein
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiTrap column chromatography and C4 reversed-phase high performance liquid chromatography
purified to homogeneity by using cation-exchange and reversed-phase chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
RPP21 and RPP29. RPP29/pET-33b plasmid transformed into Escherichia coli BL21(DE3) Rosetta cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
RNA-mediated RNA cleavage events are being increasingly exploited to disrupt RNA function, an important objective in post-genomic biology. RNase P, a ribonucleoprotein enzyme that catalyzes the removal of 5'-leaders from precursor tRNAs, has previously been utilized for sequence-specific cleavage of cellular RNAs
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wilson, R.C.; Bohlen, C.J.; Foster, M.P.; Bell, C.E.
Structure of Pfu Pop5, an archaeal RNase P protein
Proc. Natl. Acad. Sci. USA
103
873-878
2006
Pyrococcus furiosus (Q8U151)
Kawamoto, S.A.; Sudhahar, C.G.; Hatfield, C.L.; Sun, J.; Behrman, E.J.; Gopalan, V.
Studies on the mechanism of inhibition of bacterial ribonuclease P by aminoglycoside derivatives
Nucleic Acids Res.
36
697-704
2008
Escherichia coli, Methanothermobacter thermautotrophicus, Methanocaldococcus jannaschii, Pyrococcus furiosus
Tsai, H.Y.; Pulukkunat, D.K.; Woznick, W.K.; Gopalan, V.
Functional reconstitution and characterization of Pyrococcus furiosus RNase P
Proc. Natl. Acad. Sci. USA
103
16147-16152
2006
Pyrococcus furiosus
Amero, C.D.; Boomershine, W.P.; Xu, Y.; Foster, M.
Solution structure of Pyrococcus furiosus RPP21, a component of the archaeal RNase P holoenzyme, and interactions with its RPP29 protein partner
Biochemistry
47
11704-11710
2008
Pyrococcus furiosus (Q8U0H6), Pyrococcus furiosus
Xu, Y.; Amero, C.D.; Pulukkunat, D.K.; Gopalan, V.; Foster, M.P.
Solution structure of an archaeal RNase P binary protein complex: formation of the 30-kDa complex between Pyrococcus furiosus RPP21 and RPP29 is accompanied by coupled protein folding and highlights critical features for protein-protein and protein-RNA in
J. Mol. Biol.
393
1043-1055
2009
Methanocaldococcus jannaschii, Pyrococcus furiosus
Cho, I.M.; Kazakov, S.A.; Gopalan, V.
Evidence for recycling of external guide sequences during cleavage of bipartite substrates in vitro by reconstituted archaeal RNase P
J. Mol. Biol.
405
1121-1127
2011
Methanothermobacter thermautotrophicus, Methanocaldococcus jannaschii, Methanococcus maripaludis, Pyrococcus furiosus
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
Sinapah, S.; Wu, S.; Chen, Y.; Pettersson, B.M.; Gopalan, V.; Kirsebom, L.A.
Cleavage of model substrates by archaeal RNase P: role of protein cofactors in cleavage-site selection
Nucleic Acids Res.
39
1105-1116
2011
Pyrococcus furiosus
Ma, X.; Lai, L.B.; Lai, S.M.; Tanimoto, A.; Foster, M.P.; Wysocki, V.H.; Gopalan, V.
Uncovering the stoichiometry of Pyrococcus furiosus RNase P, a multi-subunit catalytic ribonucleoprotein complex, by surface-induced dissociation and Ion mobility mass spectrometry
Angew. Chem. Int. Ed. Engl.
53
11483-11487
2014
Pyrococcus furiosus
Chen, W.Y.; Pulukkunat, D.K.; Cho, I.M.; Tsai, H.Y.; Gopalan, V.
Dissecting functional cooperation among protein subunits in archaeal RNase P, a catalytic ribonucleoprotein complex
Nucleic Acids Res.
38
8316-8327
2010
Methanothermobacter thermautotrophicus, Methanocaldococcus jannaschii, Pyrococcus furiosus
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