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Information on EC 3.1.26.5 - ribonuclease P and Organism(s) Pyrococcus horikoshii and UniProt Accession O59543
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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: Pyrococcus horikoshii
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
contains catalytic RNA and the RNase P proteins PhoRpp21 and PhoRpp29
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, amino acids residues Arg90, Arg107, Lys123, Arg176, and Lys196 are involved in interaction with enzyme RNA or with the pre-tRNA
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-tRNATyr + H2O
mature tRNATyr + 5'-oligoribonucleotide
substrate from Pyrococcus horikoshii OT3, cleavage of 5'-terminal oligonucleotide
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
tRNA processing
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
the enzyme is involved in maturation of the 5'-end of tRNA
-
-
?
pre-tRNA-Tyr + H2O
tRNA-Tyr + 5'-oligoribonucleotide
-
-
-
?
pre-tRNATyr + H2O
mature tRNATyr + 5'-oligoribonucleotide
-
is completely processed. Cleaves efficiently at a single phosphodieste bond between positions U59 and C60
-
-
?
pre-tRNATyr + H2O
tRNATyr + 5' leader of tRNA
-
activity assay using in vitro reconstituted particles
-
-
?
pre-tRNA + H2O
mature tRNA + 5'-terminal oligonucleotide
-
-
-
?
pre-tRNA + H2O
mature tRNA + 5'-terminal oligonucleotide
the enzyme is involved in maturation of the 5'-end of tRNA
-
-
?
pre-tRNA(Tyr) + H2O
mature tRNA(Tyr) + 5'-terminal oligonucleotide
-
-
-
?
pre-tRNA(Tyr) + H2O
mature tRNA(Tyr) + 5'-terminal oligonucleotide
-
-
-
?
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
?
-
-
the enzyme is a ribonuleoprotein that catalyzes the processing of 5' leader sequences from tRNA precursors and other noncoding RNA
-
-
?
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
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
tRNA processing
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
the enzyme is involved in maturation of the 5'-end of tRNA
-
-
?
additional information
?
-
-
the enzyme is a ribonuleoprotein that catalyzes the processing of 5' leader sequences from tRNA precursors and other noncoding RNA
-
-
?
pre-tRNA + H2O
mature tRNA + 5'-terminal oligonucleotide
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
-
the bulge stem-loop structure containing J3/4 and helix P4 is involved in the interaction with Mg2+ ions important for catalysis
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
protein PhoPop5
the enzyme is enzymatically active only when bound to proteins PhoPop5, PhoRpp38, PhoRpp21, PhoRpp29, and PhoRpp30
-
protein PhoRpp21
the enzyme is enzymatically active only when bound to proteins PhoPop5, PhoRpp38, PhoRpp21, PhoRpp29, and PhoRpp30
-
protein PhoRpp29
the enzyme is enzymatically active only when bound to proteins PhoPop5, PhoRpp38, PhoRpp21, PhoRpp29, and PhoRpp30
-
protein PhoRpp30
the enzyme is enzymatically active only when bound to proteins PhoPop5, PhoRpp38, PhoRpp21, PhoRpp29, and PhoRpp30
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00000009
pre-tRNATyr
-
wild-type enzyme, pH not specified in the publication, 65°C
-
additional information
additional information
-
kinetics of deletion mutants
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.009
pre-tRNATyr
-
wild-type enzyme, pH not specified in the publication, 65°C
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.6
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
-
the protein subunit Ph1496p elevates the optimum temperature from 55°C (for reconstituted enzyme particles composed of RNase P RNA and four proteins: Ph1481p, Ph1601p, Ph1771p, and Ph1877p) to 70°C which is the temperature optimum of the authentic RNase P from pyrococcus horikoshii AT3
additional information
-
the deletion mutants show a slightly reduced optimal temperature compared to the wild-type enzyme
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme is involved in maturation of the 5'-end of tRNA
physiological function
additional information
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
-
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
-
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 involved in maturation of the 5'-end of tRNA
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 secondary structure of RNase P RNA is reexamined using stringent comparative tools to arrive at phylogenetically supported model. The model structure shows an essentially flat disk with 16 tightly packed helices and a conserved face suitable for the binding of pre-tRNA. The low resolution model derived from small-angle X-ray scattering and the comparative 3-D model have similar overall shapes. The 3-D model provides a framework for a better understanding of structure-function relationships of this multifaceted primordial ribozyme
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oligomer
RNase P consists of RNase P RNA (PhopRNA) and five protein cofactors designated PhoPop5, PhoRpp21, PhoRpp29, PhoRpp30, and PhoRpp38. PhoPop5 and PhoRpp30 fold into a heterotetramer and cooperate to activate a catalytic domain (C-domain) in PhopRNA, whereas PhoRpp21 and PhoRpp29 form a heterodimer and function together to activate a specificity domain (S-domain) in PhopRNA. PhoRpp38 plays a role in elevation of the optimum temperature of RNase P activity, binding to kink-turn (K-turn) motifs in two stem-loops in PhopRNA
tetramer
ribonuclease P protein component 1 (PH1771), ribonuclease P protein component 2 (PH1481), ribonuclease P protein component 3 (PH1877), ribonuclease P protein component 4 (PH1601). Three proteins Ph1481p, Ph1601p, and Ph1771p, and RNase P RNA are minimal components for the RNase P activity. However, addition of the fourth protein Ph1877p strongly stimulated enzymatic activity, indicating that all four proteins and RNase P RNA are essential for optimal RNase P activity
additional information
additional information
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
-
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
RNase P consists of a catalytic RNase P RNA (PhopRNA) and five protein cofactors designated PhoPop5, PhoRpp21, PhoRpp29, PhoRpp30, and PhoRpp38. A heterotetramer composed of PhoPop5 and PhoRpp30 bridges helices P3 and P16 in the PhopRNA C-domain, thereby probably stabilizing a double-stranded RNA structure (helix P4) containing catalytic Mg2+ ions, while a heterodimer of PhoRpp21 and PhoRpp29 locates on a single-stranded loop connecting helices P11 and P12 in the specificity domain (S-domain) in PhopRNA, probably forming an appropriate conformation of the precursor tRNA (pre-tRNA) binding site. The fifth protein PhoRpp38 binds each kink-turn motif in helices P12.1, P12.2, and P16 in PhopRNA
additional information
RNase P consists of a catalytic RNase P RNA (PhopRNA) and five protein cofactors designated PhoPop5, PhoRpp21, PhoRpp29, PhoRpp30, and PhoRpp38. A heterotetramer composed of PhoPop5 and PhoRpp30 bridges helices P3 and P16 in the PhopRNA C-domain, thereby probably stabilizing a double-stranded RNA structure (helix P4) containing catalytic Mg2+ ions, while a heterodimer of PhoRpp21 and PhoRpp29 locates on a single-stranded loop connecting helices P11 and P12 in the specificity domain (S-domain) in PhopRNA, probably forming an appropriate conformation of the precursor tRNA (pre-tRNA) binding site. The fifth protein PhoRpp38 binds each kink-turn motif in helices P12.1, P12.2, and P16 in PhopRNA
additional information
-
RNase P consists of a catalytic RNase P RNA (PhopRNA) and five protein cofactors designated PhoPop5, PhoRpp21, PhoRpp29, PhoRpp30, and PhoRpp38. A heterotetramer composed of PhoPop5 and PhoRpp30 bridges helices P3 and P16 in the PhopRNA C-domain, thereby probably stabilizing a double-stranded RNA structure (helix P4) containing catalytic Mg2+ ions, while a heterodimer of PhoRpp21 and PhoRpp29 locates on a single-stranded loop connecting helices P11 and P12 in the specificity domain (S-domain) in PhopRNA, probably forming an appropriate conformation of the precursor tRNA (pre-tRNA) binding site. The fifth protein PhoRpp38 binds each kink-turn motif in helices P12.1, P12.2, and P16 in PhopRNA
additional information
construction of a 3-D model of Pyrococcus horikoshii RNase P on the basis of crystallographic data. In the resulting 3-D structure, interactions of alpha-helices in proteins with double-stranded RNA structures appear to play an important role in stabilization of an appropriate PhopRNA conformation. Comparison of the resulting 3-D model with the crystal structure of the bacterial RNase P suggests that RNA-RNA interactions in bacterial RNase P are replaced by protein-RNA interactions in archaeal RNase P
additional information
construction of a 3-D model of Pyrococcus horikoshii RNase P on the basis of crystallographic data. In the resulting 3-D structure, interactions of alpha-helices in proteins with double-stranded RNA structures appear to play an important role in stabilization of an appropriate PhopRNA conformation. Comparison of the resulting 3-D model with the crystal structure of the bacterial RNase P suggests that RNA-RNA interactions in bacterial RNase P are replaced by protein-RNA interactions in archaeal RNase P
additional information
-
construction of a 3-D model of Pyrococcus horikoshii RNase P on the basis of crystallographic data. In the resulting 3-D structure, interactions of alpha-helices in proteins with double-stranded RNA structures appear to play an important role in stabilization of an appropriate PhopRNA conformation. Comparison of the resulting 3-D model with the crystal structure of the bacterial RNase P suggests that RNA-RNA interactions in bacterial RNase P are replaced by protein-RNA interactions in archaeal RNase P
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ribonucleoprotein
ribonucleoprotein
-
the enzyme is composed of RNA and five proteins (UniProtIDs: O59425, O59150, O59543, and O59248)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D180A
site-directed mutagenesis, activity of the holoenzyme reconstituted with the recombinant mutant protein subunit Ph1877p is unaltered compared to holoenzyme reconstituted with recombinant wild-type Ph1877p
D98A
site-directed mutagenesis, activity of the holoenzyme reconstituted with the recombinant mutant protein subunit Ph1877p is unaltered compared to holoenzyme reconstituted with recombinant wild-type Ph1877p
H114A
site-directed mutagenesis, activity of the holoenzyme reconstituted with the recombinant mutant protein subunit Ph1877p is unaltered compared to holoenzyme reconstituted with recombinant wild-type Ph1877p
K123A
site-directed mutagenesis, reconstitution of the holoenzyme with the recombinant mutant protein subunit Ph1877p results in reduced activity compared to holoenzyme reconstituted with recombinant wild-type Ph1877p
K158A
site-directed mutagenesis, activity of the holoenzyme reconstituted with the recombinant mutant protein subunit Ph1877p is unaltered compared to holoenzyme reconstituted with recombinant wild-type Ph1877p
K196A
site-directed mutagenesis, reconstitution of the holoenzyme with the recombinant mutant protein subunit Ph1877p results in reduced activity compared to holoenzyme reconstituted with recombinant wild-type Ph1877p
K42A
site-directed mutagenesis, activity of the holoenzyme reconstituted with the recombinant mutant protein subunit Ph1877p is unaltered compared to holoenzyme reconstituted with recombinant wild-type Ph1877p
R107A
site-directed mutagenesis, reconstitution of the holoenzyme with the recombinant mutant protein subunit Ph1877p results in reduced activity compared to holoenzyme reconstituted with recombinant wild-type Ph1877p
R176A
site-directed mutagenesis, reconstitution of the holoenzyme with the recombinant mutant protein subunit Ph1877p results in 78% reduced activity compared to holoenzyme reconstituted with recombinant wild-type Ph1877p
R68A
site-directed mutagenesis, reconstitution of the holoenzyme with the recombinant mutant protein subunit Ph1877p results in slightly reduced activity compared to holoenzyme reconstituted with recombinant wild-type Ph1877p
R87A
site-directed mutagenesis, activity of the holoenzyme reconstituted with the recombinant mutant protein subunit Ph1877p is unaltered compared to holoenzyme reconstituted with recombinant wild-type Ph1877p
R90A
site-directed mutagenesis, reconstitution of the holoenzyme with the recombinant mutant protein subunit Ph1877p results in reduced activity compared to holoenzyme reconstituted with recombinant wild-type Ph1877p
C68S/C71S
-
mutant enzyme exhibits little enzymatic activity, mutation in ribonuclease P protein Ph1601p
C97S/C100S
-
mutant enzyme exhibits little enzymatic activity, mutation in ribonuclease P protein Ph1601p
DELTAM1-R31
-
RNase P reconstituted with mutant protein Ph1771p has 15% reduced activity compared to that of the reconstituted RNase P with wild-type Ph1771p
E73A
mutant shows reduced activity compared to the wild type enzyme
F95A
mutant shows reduced activity compared to the wild type enzyme
K90A
mutant shows strongly reduced activity compared to the wild type enzyme
R105A
-
mutation in ribonuclease P protein Ph1601p, mutation causes a significant reduction of the reconstituted RNase P activity as compared with that reconstituted by wild-type Ph1601p
R115A
mutant shows reduced activity compared to the wild type enzyme
R75A
mutant shows reduced activity compared to the wild type enzyme
additional information
additional information
-
generation of several enzyme mutants with deleted stem loops in their RNA part. The mutants show reduced activity
additional information
-
in order to investigate their functional role, six mutants are propared, DELTAP1, DELTAP3, DELTAP8, DELTAP9, DELTAP12, and DELTAP15, in which the stem-loops including helices P1, P3, P8, P9, P12/12.1/12.2, and P15/16 are individually deleted respectively. the mutant proteins are characterized with respect to pre-tRNA cleavage activity in the presence of five proteins and also to the ability to form a complex with the proteins. The results indicate that elimination of the stem-loops results in a reduction of the pre-tRNA cleavage activity. It is further suggested that the stem-loops containing P3 or P15/16 form a binding site for the PhoPop5-PhoRpp30 complex, and that their interaction is closely involved in the structural formation of an active site in PhopRNA
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant protein subunits from Escherichia coli
ribonuclease P protein components 1, 2, 3 and 4 are expressed in Escherichia coli cells, and the resulting proteins Ph1481p, Ph1601p, Ph1771p, and Ph1877p are purified to apparent homogeneity in a set of column chromatographies. RNase P reconstituted of four proteins with the in vitro transcripted Pyrococcus horikoshii RNase P RNA exhibits enzymatic properties like those of native enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of native and selenomethionine-containing wild-type protein subunit Ph1877p, and mutant protein subunits Ph1788p in Escherichia coli
ribonuclease P protein components 1, 2, 3 and 4 are expressed in Escherichia coli cells, and the resulting proteins Ph1481p, Ph1601p, Ph1771p, and Ph1877p are purified to apparent homogeneity in a set of column chromatographies. RNase P reconstituted of four proteins with the in vitro transcripted Pyrococcus horikoshii RNase P RNA exhibits enzymatic properties like those of native enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Takagi, H.; Watanabe, M.; Kakuta, Y.; Kamachi, R.; Numata, T.; Tanaka, I.; Kimura, M.
Crystal structure of the ribonuclease P protein Ph1877p from hyperthermophilic archaeon Pyrococcus horikoshii OT3
Biochem. Biophys. Res. Commun.
319
787-794
2004
Pyrococcus horikoshii (O59543), Pyrococcus horikoshii OT-3 (O59543)
Fukuhara, H.; Kifusa, M.; Watanabe, M.; Terada, A.; Honda, T.; Numata, T.; Kakuta, Y.; Kimura, M.
A fifth protein subunit Ph1496p elevates the optimum temperature for the ribonuclease P activity from Pyrococcus horikoshii OT3
Biochem. Biophys. Res. Commun.
343
956-964
2006
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
Kakuta, Y.; Ishimatsu, I.; Numata, T.; Kimura, K.; Yao, M.; Tanaka, I.; Kimura, M.
Crystal structure of a ribonuclease P protein Ph1601p from Pyrococcus horikoshii OT3: an archaeal homologue of human nuclear ribonuclease P protein Rpp21
Biochemistry
44
12086-12093
2005
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
Kawano, S.; Nakashima, T.; Kakuta, Y.; Tanaka, I.; Kimura, M.
Crystal structure of protein Ph1481p in complex with protein Ph1877p of archaeal RNase P from Pyrococcus horikoshii OT3: implication of dimer formation of the holoenzyme
J. Mol. Biol.
357
583-591
2006
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
Numata, T.; Ishimatsu, I.; Kakuta, Y.; Tanaka, I.; Kimura, M.
Crystal structure of archaeal ribonuclease P protein Ph1771p from Pyrococcus horikoshii OT3: an archaeal homolog of eukaryotic ribonuclease P protein Rpp29
RNA
10
1423-1432
2004
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
Honda, T.; Kakuta, Y.; Kimura, K.; Saho, J.; Kimura, M.
Structure of an archaeal homolog of the human protein complex Rpp21-Rpp29 that is a key core component for the assembly of active ribonuclease P
J. Mol. Biol.
384
652-662
2008
Pyrococcus horikoshii (O59425), Pyrococcus horikoshii
Honda, T.; Hara, T.; Nan, J.; Zhang, X.; Kimura, M.
Archaeal homologs of human RNase P protein pairs Pop5 with Rpp30 and Rpp21 with Rpp29 work on distinct functional domains of the RNA subunit
Biosci. Biotechnol. Biochem.
74
266-273
2010
Escherichia coli, Pyrococcus horikoshii
Hara, T.; Terada, A.; Yamaguchi, H.; Nakashima, T.; Kakuta, Y.; Kimura, M.
The contribution of peripheral stem-loops to the catalytic activity of archaeal RNase P RNA from Pyrococcus horikoshii OT3
Biosci. Biotechnol. Biochem.
75
816-819
2011
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
Terada, A.; Yoshida, T.; Kimura, M.
Identification of nucleotide residues essential for RNase P activity from the hyperthermophilic archaeon Pyrococcus horikoshii OT3
Biosci. Biotechnol. Biochem.
71
1940-1945
2007
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
Terada, A.; Honda, T.; Fukuhara, H.; Hada, K.; Kimura, M.
Characterization of the archaeal ribonuclease P proteins from Pyrococcus horikoshii OT3
J. Biochem.
140
293-298
2006
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
Hazeyama, K.; Ishihara, M.; Ueda, T.; Nishimoto, E.; Nakashima, T.; Kakuta, Y.; Kimura, M.
Extra-structural elements in the RNA recognition motif in archaeal Pop5 play a crucial role in the activation of RNase P RNA from Pyrococcus horikoshii OT3
Biochem. Biophys. Res. Commun.
440
594-598
2013
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
Ueda, T.; Yamaguchi, H.; Miyanoshita, M.; Nakashima, T.; Kakuta, Y.; Kimura, M.
Characterization of the peripheral structures of archaeal RNase P RNA from Pyrococcus horikoshii OT3
J. Biochem.
155
25-33
2014
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
Ishihara, M.; Nishimoto, E.; Yamashita, S.; Kakuta, Y.; Kimura, M.
A distinct binding mode of archaeal ribonuclease P proteins to RNA
Biosci. Biotechnol. Biochem.
76
2335-2337
2012
Pyrococcus horikoshii
Kouzuma, Y.; Mizoguchi, M.; Takagi, H.; Fukuhara, H.; Tsukamoto, M.; Numata, T.; Kimura, M.
Reconstitution of archaeal ribonuclease P from RNA and four protein components
Biochem. Biophys. Res. Commun.
306
666-673
2003
Pyrococcus horikoshii (O59425 and O59150 and O59543 and O59248 and P62009), Pyrococcus horikoshii
Zwieb, C.; Nakao, Y.; Nakashima, T.; Takagi, H.; Goda, S.; Andersen, E.; Kakuta, Y.; Kimura, M.
Structural modeling of RNase P RNA of the hyperthermophilic archaeon Pyrococcus horikoshii OT3
Biochem. Biophys. Res. Commun.
414
517-522
2011
Pyrococcus horikoshii (O59425 and O59150 and O59543 and O59248 and P62009)
Gao, X.; Oshima, K.; Ueda, T.; Nakashima, T.; Kimura, M.
A three-dimensional model of RNase P in the hyperthermophilic archaeon Pyrococcus horikoshii OT3
Biochem. Biophys. Res. Commun.
493
1063-1068
2017
Pyrococcus horikoshii (O59150 AND O59248 AND O59425 AND O59543 AND P62009), Pyrococcus horikoshii (O59425 and O59150 and O59543 and O59248 and P62009), Pyrococcus horikoshii
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