3.1.26.5: ribonuclease P
This is an abbreviated version!
For detailed information about ribonuclease P, go to the full flat file.
Word Map on EC 3.1.26.5
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3.1.26.5
-
ribonucleoproteins
-
pre-trnas
-
endoribonuclease
-
endonucleolytic
-
eculizumab
-
aminoacylation
-
rna-based
-
stem-loops
-
phosphodiester
-
nucleolar
-
nocturnal
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eubacterial
-
paroxysmal
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gene-targeting
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anticodon
-
base-pairing
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rna-protein
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sars-cov-2
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c5a
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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
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t-loops
-
p-mediated
-
complement-mediated
-
ncrnas
-
pseudoknots
-
watson-crick
-
eukaryal
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oligoribonucleotides
-
analysis
-
pharmacology
-
snornps
-
synthesis
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medicine
-
biotechnology
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trnase
- 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
Reaction
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor =
Synonyms
Aq_880, aRpp29, aRpp29 protein, AtPop1p, AtPRORP1, AtPRORP2, AtPRORP3, C5 protein, CrPRORP, hPOP1, hPOP4, hPOP7, M1 RNA, M1GS, M1GS RNA, mitochondrial RNase P protein 1, MRPP1, MRPP2, MRPP3, nuclear ribonclease P ribonucleoprotein, nuclease, ribo-, P, Pfu Pop5, PhoPRNA, POP1, Pop1p, Pop5, Pop6, Pop7, PRORP, PRORP1, PRORP2, PRORP3, Protein C5, protein-only ribonuclease P, protein-only RNase P, protein-only RNase P enzyme, proteinaceous RNase P, ribonuclease MRP, ribonuclease P, ribonuclease P ribozyme, ribosomal RNA processing ribonucleoprotein, Ribunuclease P, RNA processing protein POP1, RNA processing protein POP5, RNA processing protein POP6, RNA processing protein POP7, RNA processing protein POP8, RNase MRP, RNase P, RNase P holoenzyme, RNase P protein, RNase P ribozyme, RNase P RNA, RNase P/MRP, RNase P/MRP protein, RNaseP protein, RNaseP protein p20, RNaseP protein p30, RNaseP protein p38, RNaseP protein p40, RNases P, RNP, Rpm2p, RPP, RPP14, Rpp20, Rpp21, Rpp25, Rpp29, Rpp30, Rpp38, RPP40, RPR, RPR1, transfer RNA 5' maturation enzyme, transfer RNA processing enzyme, tRNA processing enzyme, tRNA-processing endonuclease, tRNA-processing enzyme
ECTree
3.1.26.5 ribonuclease PAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.1.26.5 - ribonuclease P
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4.5S RNA precursor + H2O
mature 4.5S RNA + 5'-oligonucleotide
-
RNA processing
-
-
?
chloroplastic pre-tRNAPhe + H2O
chloroplastic tRNAPhe + 5' leader of tRNA
-
-
-
-
?
deproteinized pre-rRNA + H2O
mature deproteinized rRNA + 5'-oligonucleotide
-
large number of discrete cleavage sites
-
-
?
hepatitis C virus RNA + H2O
?
-
the catalytic RNase P RNA cleaves near the AUG start codon
-
-
?
mitochondrial pre-tRNACys + H2O
mitochondrial tRNACys + 5' leader of tRNA
-
-
-
-
?
pre-rRNA + H2O
?
-
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 + RNA sequence
-
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-Asp + H2O
mature tRNA-Asp + 5'-oligonucleotide
pre-tRNA-Asp from Bacillus subtilis
-
-
?
pre-tRNA-Cys + H2O
mature tRNA-Cys + 5'-oligonucleotide
pre-tRNA-Cys from Arabidopsis thaliana
-
-
?
pre-tRNA-Gly precursor + H2O
tRNA-Gly + 5'-oligoribonucleotide
analysis of the kinetics and cleavage-site selection by PRORP3 using precursor tRNAs (pre-tRNAs) with individual modifications at the canonical cleavage site, with either Rp- or Sp-phosphorothioate, or 2'-deoxy, 2'-fluoro, 2'-amino, or 2'-O-methyl substitutions. A small but robust rescue effect of Sp-phosphorothioate-modified pre-tRNA is observed in the presence of thiophilic Cd2+ ions,-consistent with metal-ion coordination to the (pro-)Sp-oxygen during catalysis. Sp-phosphorothioate, 2'-deoxy, 2'-amino, and 2'-O-methyl modification redirected the cleavage mainly to the next unmodified phosphodiester in the 5'-direction. The 2'-OH substituent at nucleotide -1 is involved in an H-bonding acceptor function. In contrast to bacterial RNase P, AtPRORP3 is able to utilize the canonical and upstream cleavage site with similar efficiency (corresponding to reduced cleavage fidelity), and the two cleavage pathways appear less interdependent than in the bacterial RNAbased system
-
-
?
pre-tRNAAla + H2O
mature tRNAAla + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide of fly substrate, hyperprocessing
generates 5'-phosphate,3'-hydroxyl-product
-
?
pre-tRNAHis + H2O
mature tRNAHis + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide of fly substrate, hyperprocessing
generates 5'-phosphate,3'-hydroxyl-product
-
?
pre-tRNAMet_ini + H2O
mature tRNAMet_ini + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide of fly initiator methionine tRNA, hyperprocessing
generates 5'-phosphate,3'-hydroxyl-product
-
?
pre-tRNATyr precursor + H2O
mature tRNATyr + 5'-terminal oligonucleotide
-
-
-
-
?
precursor tRNA + H2O
77- and 35-RNA fragments
-
ribonuclease P is the endonuclease that removes the leader fragments from the 5'-ends of precursor tRNAs
-
-
?
precursor tRNA Gly + H2O
mature tRNA Gly + 5'-GGAUUUUCCCUUUC
-
-
5' flank with homogeneous 3' end, CCAGUC-3'
-
?
tmRNA precursor + H2O
mature tmRNA + 5'-oligonucleotide
-
RNA processing
-
-
?
tRNA-like pseudoknotted structures in viral RNA + H2O
processed RNA + ?
-
tRNA-like pseudoknotted structures in viral RNA
-
-
?
tRNAPhe precursor + H2O
mature tRNAPhe + 5'-terminal oligonucleotide
-
maize tRNA substrate, structure
cleavage site determination
-
?
tRNATyr precursor + H2O
mature tRNATyr + 5'-terminal oligonucleotide
-
-
-
-
?
tRNATyrUAG precursor + H2O
?
-
RNase P cleavage of this substrate generates a 5' matured tRNA with a 7 base pair amino acceptor stem
-
-
?
4.5S RNA, precursor to + H2O
?
-
enzyme complex formed with M1 RNA from E. coli and the protein moiety from E. coli or Bacillus subtilis are active. No activity with the enzyme complex formed with M1 RNA from Bacillus subtilis and the protein from either bacterial species
-
-
?
4.5S RNA, precursor to + H2O
?
-
enzyme complex formed with M1 RNA from E. coli and the protein moiety from E. coli or Bacillus subtilis are active. No activity with the enzyme complex formed with M1 RNA from Bacillus subtilis and the protein from either bacterial species
-
-
?
4.5S RNA, precursor to + H2O
?
-
generation of the 5'-terminus of the mature molecule
-
-
?
human pre-tRNATyr + H2O
human mature tRNATyr + 5'-oligonucleotide
-
-
-
-
?
human pre-tRNATyr + H2O
human mature tRNATyr + 5'-oligonucleotide
-
-
-
-
?
pbuE adenine riboswitch + H2O
?
-
RNase P cleaves in vitro the adenine riboswitch upstream of the pbuE gene which codes for an adenine efflux pump
-
-
?
pbuE adenine riboswitch + H2O
?
-
RNase P cleaves in vitro the adenine riboswitch upstream of the pbuE gene which codes for an adenine efflux pump
-
-
?
phage f2RNA + H2O
?
-
degradation to a more limited extent than tRNA precursor
-
-
?
phage f2RNA + H2O
?
-
degradation to a more limited extent than tRNA precursor
-
-
?
phi80-induced RNA + H2O
?
-
degradation to a more limited extent than tRNA precursor
-
-
?
phi80-induced RNA + H2O
?
-
degradation to a more limited extent than tRNA precursor
-
-
?
pre-rRNA + H2O
mature rRNA
-
enzyme RNase MRP plays an important role in pre-rRNA processing
-
-
?
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
-
-
?
pre-tRNA + H2O
?
-
ribonucleoprotein enzyme required for 5'-end maturation of precursor tRNAs (pre-tRNAs)
-
-
?
pre-tRNA + H2O
mature tRNA + 5'-terminal oligonucleotide
the RNase P endonucleolytic activity is characterized by having structural but not sequence substrate requirements. This property leads to development of EGS technology, which utilizes a short antisense oligonucleotide that when forming a duplex with a target RNA induces its cleavage by RNase P
-
-
?
pre-tRNA + H2O
mature tRNA + 5'-terminal oligonucleotide
the RNase P endonucleolytic activity is characterized by having structural but not sequence substrate requirements. This property leads to development of EGS technology, which utilizes a short antisense oligonucleotide that when forming a duplex with a target RNA induces its cleavage by RNase P
-
-
?
pre-tRNA + H2O
mature tRNA + 5'-terminal oligonucleotide
-
the identity of N(-2) and N(-3) relative to the cleavage site at N(1) primarily control alternative substrate selection and act at the level of association not the cleavage step. As a consequence, the specificity for N(-1), which contacts the active site and contributes to catalysis, is suppressed
-
-
?
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 + H2O
tRNA
-
Ribonuclease P (RNase P) is a ribozyme that is responsible for thematuration of 5' termini of tRNA molecules
-
-
?
pre-tRNA + H2O
tRNA + 5' leader of tRNA
-
RNase P holoenzymes, reconstituted in vitro
-
-
?
pre-tRNA + H2O
tRNA + 5' leader of tRNA
-
RNase P holoenzymes, reconstituted in vitro
-
-
?
pre-tRNA + H2O
tRNA + 5' leader of tRNA
-
RNase P holoenzymes, reconstituted in vitro
-
-
?
pre-tRNA + H2O
tRNA + 5' leader of tRNA
-
RNase P holoenzymes, reconstituted in vitro
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
the enzyme is responsible for the cleavage of sequences from the 5' ends of precursors of tRNAs to produce the mature 5' terminus of the tRNA molecules
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
RNase P requires RNA for pre-tRNA processing. 2'-OH groups in the T stem-loop of the pre-tRNA that mediate contacts with the S-domain of the RNase P RNA
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
Chlamydomonas reinhardtii cw15 arg7-8 mt+
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
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
-
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
-
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
-
catalyzes 5' maturation of tRNAs. RNA component of RNase P is essential for pre-tRNA cleavage
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
the base at N-1 in the pre-tRNA interacts with A248 in the RNase P RNA
-
-
?
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 + H2O
tRNA + 5'-oligoribonucleotide
the enzyme is involved in maturation of the 5'-end of tRNA
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
removal of a 5' leader sequence from tRNA precursor
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
RNase P is responsible for the 5'-end maturation of precursor tRNAs
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
the enzyme is responsible for the cleavage of sequences from the 5' ends of precursors of tRNAs to produce the mature 5' terminus of the tRNA molecules
-
-
?
pre-tRNA mimic + H2O
?
-
small bipartite model substrates with different numbering of stem and 5'-flank base pairs, specific trans-cleavage at the canonical enzyme cleavage site, overview
-
-
?
pre-tRNA mimic + H2O
?
-
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 a + H2O
?
-
mimic of natural enzyme substrate consisting of a 7 bp stem and a 3 nucleotide 5'-flank
-
-
?
pre-tRNA mimic a + H2O
?
-
mimic of natural enzyme substrate consisting of a 7 bp stem and a 3 nucleotide 5'-flank
-
-
?
pre-tRNA mimic b + H2O
?
-
mimic of natural enzyme substrate consisting of a 7 bp stem and a 1 nucleotide 5'-flank
-
-
?
pre-tRNA mimic b + H2O
?
-
mimic of natural enzyme substrate consisting of a 7 bp stem and a 1 nucleotide 5'-flank
-
-
?
pre-tRNA mimic c + H2O
?
-
mimic of natural enzyme substrate consisting of a 4 bp stem and a 3 nucleotide 5'-flank
-
-
?
pre-tRNA mimic c + H2O
?
-
mimic of natural enzyme substrate consisting of a 4 bp stem and a 3 nucleotide 5'-flank
-
-
?
pre-tRNA mimic d + H2O
?
-
mimic of natural enzyme substrate consisting of a 4 bp stem and a 1 nucleotide 5'-flank
-
-
?
pre-tRNA mimic d + H2O
?
-
mimic of natural enzyme substrate consisting of a 4 bp stem and a 1 nucleotide 5'-flank
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
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
-
cleaves the G residue at the +1 position in pre-tRNAHis
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
RNA moiety can cleave pre-rRNA in buffers containing either 60 mM Mg2+ or 10 mM Mg2+ plus 1 mM spermidine
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
cleavage of pre-tRNAAsp catalyzed by circular RNase P RNA is slightly faster than with the linear form
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
the conserved sequences CCA and GUUCG, as well as the substrate bond, occur on the same face of the coaxial helix that constitutes the minimum substrate for the enzyme
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
Gln-Leu tRNA dimeric precursor from bacteriophage T4-infected E. coli
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
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
-
-
134414, 134417, 134418, 134421, 134422, 134425, 134429, 134431, 134439, 134440, 134450, 134453, 693641, 694013
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
RNA moiety can cleave pre-rRNA in buffers containing either 60 mM Mg2+ or 10 mM Mg2+ plus 1 mM spermidine
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
wild-type E. coli SuIIItRNATyr precursor
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
T4-encoded dimeric tRNA precursor
-
-
?
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
-
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
-
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
-
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
-
E. coli tRNATyr precursor
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
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
-
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
-
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
-
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
-
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
-
pre-tRNATyr
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
E. coli tRNATyr
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
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
-
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
-
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
-
pre-tRNATyr
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
E. coli tRNATyr precursor
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
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
-
cleaves the precursor to E. coli suppressor tRNATyr at the same site as E. coli RNase P
-
-
?
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
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
pre-tRNAAsp
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
pre-tRNAAsp
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
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
-
pre-tRNATyr
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
cleaves the 5'-leader sequence of precursor tRNAs during their maturation
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
E. coli tRNATyr precursor
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
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
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
Schizosaccharomyces pombe tRNA precursor derived from the sup S1 and sup3-e tRNASer genes
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
Synechocystis 6803 precursor tRNAGln
-
-
?
pre-tRNA(Tyr) + H2O
mature tRNA(Tyr) + 5'-terminal oligonucleotide
-
-
-
?
pre-tRNA(Tyr) + H2O
mature tRNA(Tyr) + 5'-terminal oligonucleotide
-
-
-
?
pre-tRNA-Ala + H2O
mature tRNA-Ala + 5'-terminal oligonucleotide
the RNA component alone shows activity on pre-tRNAala substrate at high magnesium concentrations (50 mM). The RNA and protein components associate together to manifest catalytic activity at low magnesium concentrations (20 mM). The histidine 67 in the RNR motif of RNase P protein component is important for the catalytic activity and stability of the enzyme
-
-
?
pre-tRNA-Ala + H2O
mature tRNA-Ala + 5'-terminal oligonucleotide
the RNA component alone shows activity on pre-tRNAala substrate at high magnesium concentrations (50 mM). The RNA and protein components associate together to manifest catalytic activity at low magnesium concentrations (20 mM). The histidine 67 in the RNR motif of RNase P protein component is important for the catalytic activity and stability of the enzyme
-
-
?
pre-tRNA-Gly + H2O
tRNA-Gly + 5'-oligoribonucleotide
Escherichia coli pre-tRNA-Gly
-
-
?
pre-tRNA-Gly + H2O
tRNA-Gly + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA-Gly + H2O
tRNA-Gly + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA-His + H2O
tRNA-His + 5'-oligoribonucleotide
-
-
-
?
pre-tRNA-His + H2O
tRNA-His + 5'-oligoribonucleotide
AtPRORP1 cleaves to more than 50% at the (for this tRNA) aberrant -1/+1 site to generate non-functional tRNAHis and tRNASec moieties
-
-
?
pre-tRNA-Sec + H2O
tRNA-Sec + 5'-oligoribonucleotide
-
-
-
?
pre-tRNA-Sec + H2O
tRNA-Sec + 5'-oligoribonucleotide
AtPRORP1 cleaves to more than 50% at the (for this tRNA) aberrant -1/+1 site to generate non-functional tRNAHis and tRNASec moieties
-
-
?
pre-tRNA-Tyr + H2O
tRNA-Tyr + 5'-oligoribonucleotide
-
-
-
?
pre-tRNA-Tyr + H2O
tRNA-Tyr + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNAAsp + H2O
?
-
pre-tRNA binds to RNase P using a two-step mechanism. Conformational change in the RNase P-pre-tRNA complex is coupled to the interactions between the 5' leader and P protein and aligns essential functional groups at the cleavage active site to enhance efficient cleavage of pre-tRNA
-
-
?
pre-tRNAAsp + H2O
?
-
5' fluorescein-labeled Bacillus subtilis pre-tRNAAsp (Fl-pre-tRNA) possessing a 5-nucleotide leader
-
-
?
pre-tRNAAsp + H2O
mature tRNAAsp + 5'-oligonucleotide
-
-
-
-
?
pre-tRNAAsp + H2O
tRNAAsp + 5'-oligoribonucleotide
-
5' leader segment directly interacts with P protein. The P protein binds to the 5' leader between the fourth and seventh nucleotides upstream of the cleavage site, extending the leader and decreasing its structural dynamics
-
-
?
pre-tRNAAsp + H2O
tRNAAsp + 5'-oligoribonucleotide
-
pre-tRNA binding affinities for RNase P are enhanced by sequence-specific contacts between the fourth pre-tRNA nucleotide on the 5' side of the cleavage site (N(-4)) and the RNase P protein (P protein) subunit. RNase P has a higher affinity for pre-tRNA with adenosine at N(-4), and this binding preference is amplified at physiological divalent ion concentrations. Binds A(-4) pre-tRNA 20fold more tightly than the G(-4) substrate, and binds the C(-4) and U(-4) substrates with intermediate affinity. F20 and Y34 contribute to selectivity at N(-4). The hydroxyl group of Y34 enhances selectivity, likely by forming a hydrogen bond with the N(-4) nucleotide
-
-
?
pre-tRNAAsp + H2O
tRNAAsp + 5'-oligoribonucleotide
-
pre-tRNA binding affinities for RNase P are enhanced by sequence-specific contacts between the fourth pre-tRNA nucleotide on the 5' side of the cleavage site (N(-4)) and the RNase P protein (P protein) subunit. 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-tRNATyr + H2O
mature tRNATyr + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide of human substrate, hyperprocessing
generates 5'-phosphate,3'-hydroxyl-product
-
?
pre-tRNATyr + H2O
mature tRNATyr + 5'-oligoribonucleotide
-
cleaves efficiently at a single phosphodieste bond between positions U59 and C60
-
-
?
pre-tRNATyr + H2O
mature tRNATyr + 5'-oligoribonucleotide
-
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
substrate from Pyrococcus horikoshii OT3, cleavage of 5'-terminal oligonucleotide
generates 5'-phosphate,3'-hydroxyl-product
-
?
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
mature tRNATyr + 5'-oligoribonucleotide
substrate from Pyrococcus horikoshii OT3, cleavage of 5'-terminal oligonucleotide
generates 5'-phosphate,3'-hydroxyl-product
-
?
pre-tRNATyr + H2O
mature tRNATyr + 5'-oligoribonucleotide
-
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
tRNATyr + 5' leader of tRNA
-
activity assay using in vitro reconstituted particles
-
-
?
pre-tRNATyr + H2O
tRNATyr + 5' leader of tRNA
-
activity assay using in vitro reconstituted particles
-
-
?
pre-tRNATyr + H2O
tRNATyr + 5'-oligoribonucleotide
-
pre-tRNATyr from Escherichia coli
-
-
?
pre-tRNATyr + H2O
tRNATyr + 5'-oligoribonucleotide
-
-
-
?
pre-tRNATyr + H2O
tRNATyr + 5'-oligoribonucleotide
-
pre-tRNATyr from Escherichia coli
-
-
?
pre-tRNATyr + H2O
tRNATyr + 5'-oligoribonucleotide
-
pre-tRNATyr from Escherichia coli
-
-
?
precursor tRNA + H2O
?
-
catalyze the 5' maturation of precursor tRNA
-
-
?
precursor tRNA + H2O
?
-
cleavage of precursor tRNAs with an LNA (extra methylene), 2'-OCH3, 2'-H or 2'-F modification at the canonical (c0) site by type B RNase P RNA. Extent of cleavage for the LNA (T-1) and 2'-OCH3 (T-1) substrates is extremely low. Weak cleavage of the 2'-OCH3 substrate at the c0 site. Stronger defect caused by 2'-H at nt -1 as compared to the Escherichia coli holoenzyme
-
-
?
precursor tRNA + H2O
?
-
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
?
-
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
?
-
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 + H2O
?
-
catalyzes the magnesium-dependent 5'-end maturation of tRNAs
-
-
?
ssRNA oligonucleotide + H2O
5'-phospho-3'-hydroxy-ribonucleotides
-
holoenzyme, specificity with different ssRNA substrates, determination of cleavage sites, overview
-
-
?
ssRNA oligonucleotide + H2O
5'-phospho-3'-hydroxy-ribonucleotides
-
holoenzyme, specificity with different ssRNA substrates, determination of cleavage sites, overview
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide, maturation, essential
-
-
?
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, maturation
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide, maturation, essential
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
essential enzymes in the biogenesis of tRNA, maturation
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
tRNA processing
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide, cleavage site
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
site-specific cleavage of 5'-terminal oligonucleotide from pre-tRNA, 3 potential RNA binding motifs
generates 5'-phosphate,3'-hydroxyl-product
-
?
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
-
-
?
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, maturation, essential
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
essential enzymes in the biogenesis of tRNA, maturation
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
tRNA processing
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide, cleavage site
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
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
-
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
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide, maturation, essential
-
-
?
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, maturation
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide, maturation
-
-
?
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, maturation, essential
-
-
?
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
-
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
tRNA processing
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
tRNA processing
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide, maturation
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide, maturation, essential
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
essential enzymes in the biogenesis of tRNA, maturation
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
tRNA processing, 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
-
cleavage of 5'-terminal oligonucleotide
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide, maturation
-
-
?
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
-
tRNA processing
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
site-specific cleavage of 5'-terminal oligonucleotide from pre-tRNA, 3 potential RNA binding motifs
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide, maturation, essential
-
-
?
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, maturation, essential
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNA precursor + H2O
mature tRNA + 5'-terminal oligonucleotide
-
enzyme is responsible for removing the 5'-leader segment of precursor tRNA during maturation
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-terminal oligonucleotide
-
enzyme is responsible for removing the 5'-leader segment of precursor tRNA
-
-
?
tRNAAsp precursor + H2O
mature tRNAAsp + 5'-terminal oligonucleotide
-
sequence
5'-terminal oligonucleotide with 3'-hydroxyl and 5'-phosphoryl
-
ir
tRNAAsp precursor + H2O
mature tRNAAsp + 5'-terminal oligonucleotide
-
sequence, potential catalytic transition state structure including 3 required divalent metal ions
5'-terminal oligonucleotide with 3'-hydroxyl and 5'-phosphoryl
-
ir
tRNAAsp precursor + H2O
mature tRNAAsp + 5'-terminal oligonucleotide
-
sequence
5'-terminal oligonucleotide with 3'-hydroxyl and 5'-phosphoryl
-
ir
tRNALeu5 + H2O
?
-
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
-
-
?
tRNALeu5 + H2O
?
-
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
-
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
-
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
-
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
-
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
-
?
tRNATyr precursor + H2O
mature tRNATyr + 5'-oligonucleotide
-
human substrate, cleavage of 5'-terminal oligonucleotide, enzyme recognizes the RNA substrate hairpin structure
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNATyr precursor + H2O
mature tRNATyr + 5'-oligonucleotide
-
human substrate, cleavage of 5'-terminal oligonucleotide, enzyme recognizes the RNA substrate hairpin structure
generates 5'-phosphate,3'-hydroxyl-product
-
?
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
-
?
tRNATyr precursor + H2O
mature tRNATyr + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide
generates 5'-phosphate,3'-hydroxyl-product
-
?
tRNATyr precursor + H2O
mature tRNATyr + 5'-terminal RNA oligonucleotide
-
-
-
-
?
tRNATyr precursor + H2O
mature tRNATyr + 5'-terminal RNA oligonucleotide
-
-
-
-
?
additional information
?
-
-
5'-endonucleolytic precursor tRNA cleavage
-
-
?
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
?
-
L0N807
the enzyme processes the 5'-end of tRNAs
-
-
?
additional information
?
-
the natural substrate is precursor tRNA
-
-
?
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
?
additional information
?
-
substrates are mitochondrial tRNACys precursor variants
-
-
?
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, the recognition mechanism involves the D-TpsiC loops in tRNA, overview. It is also active on Thermus thermophilus pre-tRNAGly
-
-
?
additional information
?
-
AtPRORP1 is unable to process the primary transcript of 4.5S RNA, a hairpin-like non-tRNA substrate processed by Escherichia coli RNase P
-
-
?
additional information
?
-
AtPRORP1 is unable to process the primary transcript of 4.5S RNA, a hairpin-like non-tRNA substrate processed by Escherichia coli RNase P
-
-
?
additional information
?
-
AtPRORP1 is unable to process the primary transcript of 4.5S RNA, a hairpin-like non-tRNA substrate processed by Escherichia coli RNase P
-
-
?
additional information
?
-
-
AtPRORP1 is unable to process the primary transcript of 4.5S RNA, a hairpin-like non-tRNA substrate processed by Escherichia coli RNase P
-
-
?
additional information
?
-
AtPRORP2 are essentially unable to process the primary transcript of 4.5S RNA, a hairpin-like non-tRNA substrate processed by Escherichia coli RNase P
-
-
?
additional information
?
-
AtPRORP2 are essentially unable to process the primary transcript of 4.5S RNA, a hairpin-like non-tRNA substrate processed by Escherichia coli RNase P
-
-
?
additional information
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AtPRORP2 are essentially unable to process the primary transcript of 4.5S RNA, a hairpin-like non-tRNA substrate processed by Escherichia coli RNase P
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additional information
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AtPRORP2 are essentially unable to process the primary transcript of 4.5S RNA, a hairpin-like non-tRNA substrate processed by Escherichia coli RNase P
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additional information
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AtPRORP3 is unable to process the primary transcript of 4.5S RNA, a hairpin-like non-tRNA substrate processed by Escherichia coli RNase P
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additional information
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AtPRORP3 is unable to process the primary transcript of 4.5S RNA, a hairpin-like non-tRNA substrate processed by Escherichia coli RNase P
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?
additional information
?
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AtPRORP3 is unable to process the primary transcript of 4.5S RNA, a hairpin-like non-tRNA substrate processed by Escherichia coli RNase P
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?
additional information
?
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AtPRORP3 is unable to process the primary transcript of 4.5S RNA, a hairpin-like non-tRNA substrate processed by Escherichia coli RNase P
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additional information
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RNase P cleaves transient structures in some riboswitches
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additional information
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other pre-RNAs are also physiological substrates of the enzyme
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additional information
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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
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additional information
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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
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additional information
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structural basis and mechanism of substrate specificity, global structure of the enzyme-substrate complex
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additional information
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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
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additional information
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substrate requirements for trans-cleavage of wild-type and mutant hybrid enzymes, overview
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additional information
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the RNA subunit can cleave tRNA substrate in absence of the protein subunit
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additional information
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catalyzes the 5-end maturation of tRNAs in all Kingdoms of life
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additional information
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the guanine riboswitch encoded upstream of xpt-pbuX operon, is not cleaved
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additional information
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5'-endonucleolytic precursor tRNA cleavage
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additional information
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ribonuclease P catalyzes the metal-dependent 5' end maturation of precursor tRNAs
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additional information
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the enzyme catalyzes the 5' end maturation of precursor tRNAs (pre-tRNAs)
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additional information
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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
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additional information
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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
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additional information
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the guanine riboswitch encoded upstream of xpt-pbuX operon, is not cleaved
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additional information
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other pre-RNAs are also physiological substrates of the enzyme
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additional information
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hyperprocessing occurs with tRNA molecules denatured to form double-hair pin-like structures, instead of cloverleaf structure, reaction mechanism
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additional information
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structural basis and mechanism of substrate specificity, global structure of the enzyme-substrate complex
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additional information
?
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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
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additional information
?
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substrate requirements for trans-cleavage of wild-type and mutant hybrid enzymes, overview
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additional information
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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
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additional information
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the RNA subunit is the catalytic subunit, while the protein subunits are essential for substrate binding, broad substrate specificity
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additional information
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catalytic RNase P RNA does not cleave hepatitis C virus RNA
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?
additional information
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RNase P cleaves transient structures in some riboswitches
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?
additional information
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catalyses the 5'-end processing reaction of tRNA precursor molecules
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additional information
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essential ribonucleoprotein enzyme responsible for the 5'-end maturation of tRNAs
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additional information
?
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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5'-endonucleolytic precursor tRNA cleavage
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additional information
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precursor tRNAs are natural enzyme RNase P substrates
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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?
additional information
?
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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
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additional information
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substrate is a RNA-tRNA primary transcript
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additional information
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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)
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additional information
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usage of model hairpin loop RNA substrates, e.g. pMini3bpUG, pATSerCG or pATSerUG, secondary structures, overview
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additional information
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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
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additional information
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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
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additional information
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protein subunit Rpp20 also acts as an ATPase, protein subunits Rpp14, Rpp21, and Rpp29 are responsible for pre-tRNA substrate binding
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additional information
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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
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additional information
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recognition of bipartite substrates and chimera constructed from external guide sequences EGS and ssRNA
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additional information
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substrate specificities of enzyme forms RNase P and RNase MRP
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additional information
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the recombinant holoenzyme and the Rpp20p subunit display ATPase activity
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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phylogenetic study of archeal enzymes
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additional information
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5-maturation of transfer RNA
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additional information
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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
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additional information
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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
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additional information
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phylogenetic study of archeal enzymes
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additional information
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5-maturation of transfer RNA
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additional information
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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
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additional information
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external guide sequences EGS can bind to complementary sequence of substrate ssRNA and thereby target the enzyme to specific cleavage sites
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additional information
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M1GS RNA cleaves the overlapping mRNA region of two murine cytomegalovirus capsid proteins essential for viral replication: the assembly protein (mAP) and M80
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additional information
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the natural substrate is precursor tRNA
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additional information
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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
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additional information
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essential ribonucleoprotein enzyme responsible for the 5'-end maturation of tRNAs
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?
additional information
?
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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
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additional information
?
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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
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additional information
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the enzyme is a ribonuleoprotein that catalyzes the processing of 5' leader sequences from tRNA precursors and other noncoding RNA
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additional information
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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
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additional information
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coordination of RNA pathways, overview
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additional information
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the mitochondrial ribozyme RNA subunit might have a cellular function outside the mitochondria
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additional information
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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
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additional information
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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
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additional information
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substrate specificities of enzyme forms RNase P and RNase MRP
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additional information
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involved in regulation of noncoding RNA (ncRNA) expression
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additional information
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yeast RNase P may process antisense RNAs from genes encoding ribosomal proteins
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additional information
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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
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additional information
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the natural substrate is precursor tRNA
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additional information
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structures of the acceptor stem and anticodon/intron loop of the tRNA are crucial for Schizosaccharomyces pombe RNase P action
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additional information
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assay substrate is tobacco chloroplast precursor tRNAGly
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additional information
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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
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?
additional information
?
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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
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?
additional information
?
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the RNA subunit is the catalytic subunit, while the protein subunits are essential for substrate binding, broad substrate specificity
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?
additional information
?
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cleaves the internal ribosome entry site region in hepatitis C virus RNA near the AUG start codon
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?
additional information
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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
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additional information
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the enzyme is an RNA-based enzyme primarily catalyzing 5'-end pre-tRNA processing
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additional information
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the enzyme is an RNA-based enzyme primarily catalyzing 5'-end pre-tRNA processing
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additional information
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the natural substrate is precursor tRNA
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additional information
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the enzyme PRORP1 cleaves pre-tRNAs substrates lacking an anticodon arm,n recognition mechanism involves the D-TpsiC loops in tRNA, overview
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additional information
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essential ribonucleoprotein enzyme responsible for the 5'-end maturation of tRNAs
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additional information
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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
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additional information
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5'-endonucleolytic precursor tRNA cleavage
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additional information
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substrate is a RNA-tRNA primary transcript
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additional information
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the enzyme processes the 5'-end of tRNAs
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additional information
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substrate used in assays is Escherichia coli pre-tRNATyr
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additional information
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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
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additional information
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RNase P is the endonuclease that removes 5' extensions from tRNA precursors
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additional information
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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
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