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endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
-
-
-
-
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 structure-function study, substrate recognition and catalytic mechanism of the ribozyme
-
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 structure-function study, substrate recognition and catalytic mechanism of the ribozyme
-
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
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, chloroplast enzyme does not use the ribozyme-type pre-tRNA cleavage mechanism, distinct from bacterial reaction mechanism
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, cleavage of ssRNA, mechanism
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, cleavage of ssRNA, mechanism
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, conserved residues in J5/15 are responsible for substrate affinity and specificity of the ribozyme, nucleotide base N(-1) is involved in substrate recognition in bacteria and archea
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, non-RNA-based cleavage mechanism, structure-function relationship of eukaryotic enzymes
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, reaction mechanism in 3 consecutive steps: pre-tRNA binding, hydrolysis of the scissile phosphodiester bond, generating a 3'-hydroxyl and a 5'-phosphate group, possibly via a trigonal bipyramide, intermediate, and the dissociation of the mature tRNA and the 5'-leader product, structure-function relationship of eukaryotic enzymes
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, reaction mechanism in 3 consecutive steps: pre-tRNA binding, hydrolysis of the scissile phosphodiester bond, generating a 3'-hydroxyl and a 5'-phosphate group, possibly via a trigonal bipyramide, intermediate, and the dissociation of the mature tRNA and the 5'-leader product, substrate recognition mechanism, overview, structure-function realtionship of eukaryotic enzymes
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, RNA-based catalytic mechanism
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, secondary structural features, e.g. helix P4, sequence J5/15 or J18/2 in the RNA portion of the enzyme, are important for catalysis
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, structure-function study, substrate recognition and catalytic mechanism of the ribozyme
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, substrate recognition mechanism, detection methods, the RNA and protein subunits cooperate to bind different portions of the substrate structure, with the RNA subunit predominantly interacting with the mature domain of tRNA and the protein interacting with the 5'-leader sequence, substrate recognition and binding, reaction mechanism and detection methods
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, substrate recognition, enzyme possesses a single-stranded RNA binding cleft that interacts with the unpaired 5'-leader
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, the protein subunit is essential for substrate binding, the RNA subunit is essential for catalysis
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, the protein subunit is essential for substrate binding, the RNA subunit is essential for catalysis
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, the RNA subunit is essential for catalytic activity, divalent metal ion-dependent in-line SN2 displacement mechanism
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, the RNA subunit is essential for catalytic activity, divalent metal ion-dependent in-line SN2 displacement mechanism
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, the RNA subunit is essential for catalytic activity, divalent metal ion-dependent in-line SN2 displacement mechanism
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, the RNA subunit is essential for catalytic activity, divalent metal ion-dependent in-line SN2 displacement mechanism
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, the RNA subunit is essential for catalytic activity, divalent metal ion-dependent in-line SN2 displacement mechanism
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, the RNA subunit is essential for catalytic activity, divalent metal ion-dependent in-line SN2 displacement mechanism
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, the RNA subunit is essential for catalytic activity, except for the mitochondrial enzyme, divalent metal ion-dependent in-line SN2 displacement mechanism
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, the RNA subunit is the catalytic unit, while protein subunit Rpp25 is involved in RNA substrate binding, both interact with each other
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, tRNA precursor substrate recognition and cleavage mechanism
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, tRNA precursor substrate recognition and cleavage mechanism
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, tRNA precursor substrate recognition and cleavage mechanism
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, tRNA precursor substrate recognition and cleavage mechanism
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, tRNA precursor substrate recognition and cleavage mechanism
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, tRNA precursor substrate recognition and cleavage mechanism, CR-IV region is imporatnt for tRNA binding
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, tRNA precursor substrate recognition and cleavage mechanism, CR-IV region is important for tRNA binding
-
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, tRNA precursor substrate recognition and cleavage mechanism, structure-function relationship of the RNA subunit
-
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
-
-
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10Sa RNA + H2O
?
-
-
-
-
?
4.55 rRNA precursor + H2O
mature 4.55 rRNA + 5'-oligonucleotide
-
-
-
-
?
4.5S RNA precursor + H2O
mature 4.5S RNA + 5'-oligonucleotide
-
RNA processing
-
-
?
4.5S RNA, precursor to + H2O
?
C4 antisense RNA + H2O
?
-
from bacteriophages P1 and P7
-
-
?
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
-
-
?
human pre-tRNATyr + H2O
human mature tRNATyr + 5'-oligonucleotide
influenza virus mRNA + H2O
?
mitochondrial pre-tRNACys + H2O
mitochondrial tRNACys + 5' leader of tRNA
-
-
-
-
?
pbuE adenine riboswitch + H2O
?
phage antisense RNA (C4) + H2O
?
-
-
-
-
?
phi80-induced RNA + H2O
?
polycistronic his operon mRNA precursor + H2O
?
-
-
-
-
?
polycistronic mRNA precursor + H2O
mature mRNAs + ?
-
RNA processing
-
-
?
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-rRNA + H2O
mature rRNA
pre-rRNA + H2O
mature rRNA + 5'-oligonucleotide
-
RNase MRP
-
-
?
pre-tRNA + H2O
mat-tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
mature tRNA + 5'-oligonucleotide
-
-
-
-
?
pre-tRNA + H2O
mature tRNA + 5'-terminal oligonucleotide
pre-tRNA + H2O
tRNA + 5' leader of tRNA
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
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 precursor + H2O
mat-tRNA + RNA
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
pre-tRNA supS1 tRNASer + H2O
?
-
-
-
-
?
pre-tRNA(Tyr) + H2O
mature tRNA(Tyr) + 5'-terminal oligonucleotide
pre-tRNA-Ala + H2O
mature tRNA-Ala + 5'-terminal oligonucleotide
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 + H2O
tRNA-Gly + 5'-oligoribonucleotide
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-tRNA-His + H2O
tRNA-His + 5'-oligoribonucleotide
pre-tRNA-Met + H2O
tRNA-Met + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA-Sec + H2O
tRNA-Sec + 5'-oligoribonucleotide
pre-tRNA-Tyr + H2O
tRNA-Tyr + 5'-oligoribonucleotide
pre-tRNA-Val + H2O
tRNA-Val + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA3Pro + H2O
mature tRNA3Pro + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNAAla + H2O
mature tRNAAla + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide of fly substrate, hyperprocessing
generates 5'-phosphate,3'-hydroxyl-product
-
?
pre-tRNAAsp + H2O
mature tRNAAsp + 5'-oligonucleotide
pre-tRNAAsp + H2O
tRNAAsp + 5'-oligoribonucleotide
pre-tRNAHis + H2O
mature tRNAHis + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide of fly substrate, hyperprocessing
generates 5'-phosphate,3'-hydroxyl-product
-
?
pre-tRNALeu + H2O
tRNALeu + 5' leader of tRNA
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-tRNAPhe + H2O
?
-
-
-
?
pre-tRNAPhe + H2O
tRNAPhe + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNATyr + H2O
mature tRNATyr + 5'-oligonucleotide
pre-tRNATyr + H2O
mature tRNATyr + 5'-oligoribonucleotide
pre-tRNATyr + H2O
tRNATyr + 5' leader of tRNA
pre-tRNATyr + H2O
tRNATyr + 5'-oligoribonucleotide
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'
-
?
precursors to 4.5S RNA + H2O
?
-
-
-
-
?
ssRNA oligonucleotide + H2O
5'-phospho-3'-hydroxy-ribonucleotides
SupS1 precursor + H2O
?
-
-
-
-
?
syntaxin18 mRNA + H2O
?
-
-
-
-
?
tmRNA precursor + H2O
mature tmRNA + 5'-oligonucleotide
-
RNA processing
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
tRNA precursor + H2O
mature tRNA + 5'-terminal oligonucleotide
tRNA-like pseudoknotted structures in viral RNA + H2O
processed RNA + ?
-
tRNA-like pseudoknotted structures in viral RNA
-
-
?
tRNAAsp precursor + H2O
mature tRNAAsp + 5'-terminal oligonucleotide
tRNAPhe (A+1) precursor + H2O
mature tRNAPhe + 5'-terminal oligonucleotide
tRNAPhe (G+1) precursor + H2O
mature tRNAPhe + 5'-terminal oligonucleotide
tRNAPhe precursor + H2O
mature tRNAPhe + 5'-terminal oligonucleotide
-
maize tRNA substrate, structure
cleavage site determination
-
?
tRNATyr precursor + H2O
mature tRNATyr + 5'-oligonucleotide
tRNATyr precursor + H2O
mature tRNATyr + 5'-terminal oligonucleotide
-
-
-
-
?
tRNATyr precursor + H2O
mature tRNATyr + 5'-terminal RNA oligonucleotide
tRNATyrUAG precursor + H2O
?
-
RNase P cleavage of this substrate generates a 5' matured tRNA with a 7 base pair amino acceptor stem
-
-
?
additional information
?
-
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
?
-
-
-
-
?
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
-
-
-
-
?
influenza virus mRNA + H2O
?
-
-
-
-
?
influenza virus mRNA + H2O
?
-
cells transfected with virus
-
-
?
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-rRNA + H2O
mature rRNA
-
RNase MRP
-
-
?
pre-tRNA + H2O
?
-
in mitochondria, RNase P function has been taken over by an unrelated, protein-only enzyme activity
-
-
?
pre-tRNA + H2O
?
-
-
-
-
?
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
-
-
-
-
?
pre-tRNA + H2O
mature tRNA + 5'-terminal oligonucleotide
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5' leader of tRNA
-
RNase P holoenzymes, reconstituted in vitro
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
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
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
Chlamydomonas reinhardtii cw15 arg7-8 mt+
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
Mesomycoplasma mobile
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
the enzyme is involved in maturation of the 5'-end of tRNA
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
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
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
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
-
pre-tRNATyr
-
-
ir
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
Synechocystis 6803 precursor tRNAGln
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
pre-tRNATyr
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA precursor + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
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-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-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
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-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-tRNAAsp + H2O
tRNAAsp + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNALeu + H2O
tRNALeu + 5' leader of tRNA
-
-
-
?
pre-tRNALeu + H2O
tRNALeu + 5' leader of tRNA
-
-
-
?
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'-oligonucleotide
-
-
-
-
?
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' leader of tRNA
-
-
-
-
?
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
-
-
?
ptRNATyr + H2O
?
-
from Escherichia coli
-
-
?
ptRNATyr + H2O
?
-
from Eschericha coli
-
-
?
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
-
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, 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
-
-
-
-
?
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
?
-
-
catalyze tRNA 5-end maturation
-
-
?
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
?
-
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
?
-
AtPRORP3 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
?
-
AtPRORP3 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
?
-
AtPRORP3 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
?
-
-
AtPRORP3 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
?
-
-
RNase P cleaves transient structures in some riboswitches
-
-
?
additional information
?
-
-
other pre-RNAs are also physiological substrates of the enzyme
-
-
?
additional information
?
-
-
substrate specificity is determined by the enzymes' RNA fold, the structure of the specificity domain of the RNA subunit provides the basis of understanding the structurs of other bacterial ribozyme molecules because all bacterial S domains havea common core that comprises stems P7-P11 plus J11/12-J12/11 module, overview
-
-
?
additional information
?
-
-
enzymatic and chemical protection, cross-linking of enzyme and substrate for determination of binding features, overview, the RNA subunit is the catalytic subunit, while the protein subunits are essential for substrate binding, broad substrate specificity
-
-
?
additional information
?
-
-
structural basis and mechanism of substrate specificity, global structure of the enzyme-substrate complex
-
-
?
additional information
?
-
-
substitution of a sulfur atom for either the Rp or Sp nonbridging phosphate oxygen or the 3'oxyanion leaving group in pre-tRNA decreases the catalytic rate constant by over 1000fold
-
-
?
additional information
?
-
-
substrate requirements for trans-cleavage of wild-type and mutant hybrid enzymes, overview
-
-
?
additional information
?
-
-
the RNA subunit can cleave tRNA substrate in absence of the protein subunit
-
-
?
additional information
?
-
-
catalyzes the 5-end maturation of tRNAs in all Kingdoms of life
-
-
?
additional information
?
-
-
the guanine riboswitch encoded upstream of xpt-pbuX operon, is not cleaved
-
-
?
additional information
?
-
-
cleaves riboswitchs
-
-
?
additional information
?
-
-
5'-endonucleolytic precursor tRNA cleavage
-
-
?
additional information
?
-
-
ribonuclease P catalyzes the metal-dependent 5' end maturation of precursor tRNAs
-
-
?
additional information
?
-
-
the enzyme catalyzes the 5' end maturation of precursor tRNAs (pre-tRNAs)
-
-
?
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
?
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
?
-
-
the enzyme catalyzes the 5' end maturation of precursor tRNAs (pre-tRNAs). Inner-sphere coordination of divalent metal ions to PRNA is essential for catalytic activity, but not for the formation of the RNase P-pre-tRNA complex, which undergoes an essential conformational change before the cleavage step
-
-
?
additional information
?
-
-
the guanine riboswitch encoded upstream of xpt-pbuX operon, is not cleaved
-
-
?
additional information
?
-
-
the RNA subunit alone is not active
-
-
?
additional information
?
-
-
other pre-RNAs are also physiological substrates of the enzyme
-
-
?
additional information
?
-
-
hyperprocessing occurs with tRNA molecules denatured to form double-hair pin-like structures, instead of cloverleaf structure, reaction mechanism
-
-
?
additional information
?
-
-
structural basis and mechanism of substrate specificity, global structure of the enzyme-substrate complex
-
-
?
additional information
?
-
-
substitution of a sulfur atom for either the Rp or Sp nonbridging phosphate oxygen or the 3'oxyanion leaving group in pre-tRNA decreases the catalytic rate constant by over 1000fold
-
-
?
additional information
?
-
-
substrate requirements for trans-cleavage of wild-type and mutant hybrid enzymes, overview
-
-
?
additional information
?
-
-
targeting of any mRNA for cleavage by the enzyme with aid of external guide sequences EGS, e.g. EGS with chloramphenicol acetyltransferase mRNA from cat, or EGS with gyrase A mRNA from Salmonella typhimurium, forming a complex with the complementary RNA substrate sequence, overview
-
-
?
additional information
?
-
-
the RNA subunit is the catalytic subunit, while the protein subunits are essential for substrate binding, broad substrate specificity
-
-
?
additional information
?
-
-
catalytic RNase P RNA does not cleave hepatitis C virus RNA
-
-
?
additional information
?
-
-
RNase P cleaves transient structures in some riboswitches
-
-
?
additional information
?
-
-
5'-maturation of transfer RNA
-
-
?
additional information
?
-
-
catalyses the 5'-end processing reaction of tRNA precursor molecules
-
-
?
additional information
?
-
-
essential ribonucleoprotein enzyme responsible for the 5'-end maturation of tRNAs
-
-
?
additional information
?
-
-
RNase P cleaves the mRNAs of Yersinia pestis yscN and yscS genes in vitro with the cognate external guide sequences resulting in the reduction of the levels of these messages of the virulence genes when those genes are expressed in Escherichia coli
-
-
?
additional information
?
-
-
cleaves riboswitchs
-
-
?
additional information
?
-
-
interaction of immobilized RNase P protein and 3'-biotinylated RNase P RNA bound to streptavidin-coated magnetic beads. The protein binds to the C-domain of P RNA in the P2-J2/3-P3-J3/4-P4-J18/2 region. Kd values of about 1-2 nanomol (at 4.5 mM Mg2+ and 150 mM NH4+) for RNase P RNA and protein. A bacterial-like 1-bp insertion and 2-nt deletion in the helix P2/P3 region largely improves affinity, thus these elements are crucial for interaction of the two RNase P subunits
-
-
?
additional information
?
-
-
is unable to activate non-cognate RNase P RNAs, Pyrococcus horikoshii RNase P RNA and Escherichia coli RNase P RNA. Chimeric RNase P RNAs composed of the Escherichia coli RNA C-domain and Pyrococcus horikoshii S-domain or composed of the Pyrococcus horikoshii C-domain and Escherichia coli RNA S-domain, respectively, exhibit activity. C5 protein is involved in activation of the Escherichia coli pRNA C-domain
-
-
?
additional information
?
-
-
M1GSs directed against BCR-ABL chimeric RNAs are efficient in specifically cleaving the chimeric RNA transcripts. M1GS directed against the thymidine kinase mRNA from herpes simplex virus 1 is able to reduce the thymidine kinase mRNA and protein level with 80%. Efficiency of inhibition can be improved to above 90% reduction in mRNA and protein level, and 4000fold reduction in herpes simplex virus 1 viral load, using an M1GS ribozyme optimized through in vitro selection
-
-
?
additional information
?
-
-
5'-endonucleolytic precursor tRNA cleavage
-
-
?
additional information
?
-
-
precursor tRNAs are natural enzyme RNase P substrates
-
-
?
additional information
?
-
-
the enzyme processes the 5' ends of tRNA precursors, the substrate population includes over 80 different competing ptRNAs in Escherichia coli, sequence and secondary structure of representative ptRNAs, overview. Its mode of molecular recognition differs from other catalytic RNAs in two important ways. First, its biological role in ptRNA processing requires that it act in trans as a multiple turnover enzyme, whereas other ribozymes, with the exceptions of the ribosome and spliceosome, undergo single turnover self-splicing or self-cleavage reactions. Second, RNase P processes multiple RNA substrates, including all ptRNAs in the cell, whereas other ribozymes, again with the exceptions of the ribosome and spliceosome, have one specific substrate
-
-
?
additional information
?
-
-
the mechanism by which the enzyme processes the valU and lysT polycistronic transcripts (valV valW, valU valX, valY lysY and lysT valT lysW valZ lysY lysZ lysQ) involves initiation of processing by first endonucleolytically removing the Rho-independent transcription terminators from the primary valU and lysT transcripts. Subsequently, the enzyme proceeds in the 3' -> 5' direction generating one pre-tRNA at a time. Identification of cleavage sites using RNA circularization, overview
-
-
?
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
?
additional information
?
-
-
construction of a modell substrate for M1 RNA from Escherichia coli. wild-type and mutant enzymes cleave the HIV RNA sequence in the tat region. The variant, containing combined mutations at nucleotide 83 and 340 of RNase P catalytic RNA, cleaves the tat RNA sequence in vitro about 20 times more efficiently than the wild-type ribozyme
-
-
?
additional information
?
-
-
in vitro, bacterial P RNA can catalyze tRNA maturation in the absence of the protein cofactor at elevated concentrations of mono- and divalent cations, thus acting as a trans-acting multiple-turnover ribozyme. Dissociation of the tRNA product from the catalytic RNA usually limits the rate of the RNA-alone reaction under multiple-turnover conditions
-
-
?
additional information
?
-
-
method development for the engineered catalytic RNA subunit of Escherichia coli RNase P to cleave tRNA-like substrates and other target RNAs, including specific mRNAs, detailed overview
-
-
?
additional information
?
-
-
substrate is a RNA-tRNA primary transcript
-
-
?
additional information
?
-
-
the ptRNA substrates are 5'-end-labeled with [gamma-32P]ATP and T4 polynucleotide kinase, after dephosphorylation by alkaline phosphatase, in reaction with RNase P holoenzyme
formation of products from two substrates independently in the same reaction, ptRNAfMet47 and ptRNAMet82 are modified for eparation by PAGE by the addition of two extra G nucleotides to the 5' end of the leader sequence, giving rise to ptRNAfMet47(+2) and ptRNAMet82(+2)
-
?
additional information
?
-
-
usage of model hairpin loop RNA substrates, e.g. pMini3bpUG, pATSerCG or pATSerUG, secondary structures, overview
-
-
?
additional information
?
-
-
the mechanism by which the enzyme processes the valU and lysT polycistronic transcripts (valV valW, valU valX, valY lysY and lysT valT lysW valZ lysY lysZ lysQ) involves initiation of processing by first endonucleolytically removing the Rho-independent transcription terminators from the primary valU and lysT transcripts. Subsequently, the enzyme proceeds in the 3' -> 5' direction generating one pre-tRNA at a time. Identification of cleavage sites using RNA circularization, overview
-
-
?
additional information
?
-
-
biosynthesis and regulation of RNase P, transient interactions with several proteins in the cell, the protein subunits are conserved between RNase P and RNase MRP, and are essential for cell viability and enzyme function, overview, enzyme subunits in nucleolus and Cajal bodies might be involved in cell mitosis and cell-cycle-dependent gene transcription
-
-
?
additional information
?
-
-
coordination of RNA pathways, overview
-
-
?
additional information
?
-
-
protein subunit Rpp20 also acts as an ATPase, protein subunits Rpp14, Rpp21, and Rpp29 are responsible for pre-tRNA substrate binding
-
-
?
additional information
?
-
-
protein subunits Rpp21 and Rpp29 and RNA subunit H1 are sufficient for effective substrate cleavage, thereby the protein subunits facilitate catalytic activity of RNA subunit H1 which requires a phylogenetically conserved pseudoknot-structure for function, protein subunit Rpp29 formsa catalytic complex with M1 RNA from Escherichia coli
-
-
?
additional information
?
-
-
recognition of bipartite substrates and chimera constructed from external guide sequences EGS and ssRNA
-
-
?
additional information
?
-
-
substrate specificities of enzyme forms RNase P and RNase MRP
-
-
?
additional information
?
-
-
the recombinant holoenzyme and the Rpp20p subunit display ATPase activity
-
-
?
additional information
?
-
-
the human mitochondrial RNase P is an entirely protein-based enzyme, protein MRPP1, a probable tRNA methylase, provides tRNA-binding specificity to the RNase P enzyme, protein MRPP2 binds tightly to MRPP1 and is a member of the short chain dehydrogenase/reductase protein family, protein MRPP3 may provide the enzymatic cleavage activity for the patchwork enzyme
-
-
?
additional information
?
-
-
cleavage of target RNA by RNase P is induced when three-fourths of a tRNA is used as an external guide sequence. RNase P enzyme seems to have lost the RNA component during evolution, proving that the catalytic activity of the RNA component of the RNase P holoenzyme can be accomplished by proteins alone. RNase P is able to cleave a model substrate containing only the acceptor stem, a 1 nucleotide (A or C) bulge and the T stem-loop. Cleavage of target RNAs is enhanced if the external guide sequence also contains a variable loop and form a D-like stem with the target, as a minimized 3/4 external guide sequence. Cleaves the internal ribosome entry site region in hepatitis C virus RNA. RNase P-mediated inhibition of mRNAs involved in cancer
-
-
?
additional information
?
-
-
Rpp20 and Rpp25 interact with the P3 arm of RNase MRP RNA in a highly synergic fashion. Rpp20 and Rpp25 interact with the P3 RNA as a heterodimer, which is formed prior to RNA binding
-
-
?
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
?
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
?
additional information
?
-
-
constructed substrate: a hybridized complex of an external guide sequence and a target RNA, e.g. mRNA, that resembles the structure of a tRNA, structure overview
-
-
?
additional information
?
-
-
phylogenetic study of archeal enzymes
-
-
?
additional information
?
-
-
5-maturation of transfer RNA
-
-
?
additional information
?
-
-
an external guide sequence, EGS, RNA base-paired to a target RNA makes the latter a substrate for endogenous RNase P by rendering the bipartite target RNA-EGS complex a precursor tRNA structural mimic. RNase P holoenzymes recognize and cleave such substrate-EGS complexes. The external guide sequences engage in multiple rounds of substrate recognition while assisting archaeal RNase P-mediated cleavage of a target RNA in vitro
-
-
?
additional information
?
-
-
an external guide sequence, EGS, RNA base-paired to a target RNA makes the latter a substrate for endogenous RNase P by rendering the bipartite target RNA-EGS complex a precursor tRNA structural mimic. RNase P holoenzymes recognize and cleave such substrate-EGS complexes. The external guide sequences engage in multiple rounds of substrate recognition while assisting archaeal RNase P-mediated cleavage of a target RNA in vitro
-
-
?
additional information
?
-
-
phylogenetic study of archeal enzymes
-
-
?
additional information
?
-
-
5-maturation of transfer RNA
-
-
?
additional information
?
-
-
an external guide sequence, EGS, RNA base-paired to a target RNA makes the latter a substrate for endogenous RNase P by rendering the bipartite target RNA-EGS complex a precursor tRNA structural mimic. RNase P holoenzymes recognize and cleave such substrate-EGS complexes. The external guide sequences engage in multiple rounds of substrate recognition while assisting archaeal RNase P-mediated cleavage of a target RNA in vitro
-
-
?
additional information
?
-
-
external guide sequences EGS can bind to complementary sequence of substrate ssRNA and thereby target the enzyme to specific cleavage sites
-
-
?
additional information
?
-
-
M1GS RNA cleaves the overlapping mRNA region of two murine cytomegalovirus capsid proteins essential for viral replication: the assembly protein (mAP) and M80
-
-
?
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
?
additional information
?
-
-
expression validated by Northern blotting, transcription initiation sites mapped by primer extension and RNase protection assay, secondary structure deduced, longer and more complex P3 helix-loop-helix structures compared to vertebrates
-
-
?
additional information
?
-
-
essential ribonucleoprotein enzyme responsible for the 5'-end maturation of tRNAs
-
-
?
additional information
?
-
-
5-maturation of transfer RNA
-
-
?
additional information
?
-
-
an external guide sequence, EGS, RNA base-paired to a target RNA makes the latter a substrate for endogenous RNase P by rendering the bipartite target RNA-EGS complex a precursor tRNA structural mimic. RNase P holoenzymes recognize and cleave such substrate-EGS complexes. The external guide sequences engage in multiple rounds of substrate recognition while assisting archaeal RNase P-mediated cleavage of a target RNA in vitro
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
interaction of four RNase P proteins (Pop5, Rpp21, Rpp29 and Rpp30) with RNase P RNA results in destabilization of base stacking in RNase P RNA, wheras addition of a fifth protein (Rpp38) increases base stacking of RNase P RNA
-
-
?
additional information
?
-
-
coordination of RNA pathways, overview
-
-
?
additional information
?
-
-
the mitochondrial ribozyme RNA subunit might have a cellular function outside the mitochondria
-
-
?
additional information
?
-
-
transient interactions with several proteins in the cell, e.g. protein subunit Rpp20 interacts with the heat shock protein Hsp27, protein subunit Rpp14 interacts with several proteins including the LIM domain protein 1 LIMD1 and the SR-rich HSPC232
-
-
?
additional information
?
-
-
no activity with substrates in which the pro-Rp or pro-Sp nonbridging oxygen of the scissile bond is replaced by sulfur, substitution via phosphothionate
-
-
?
additional information
?
-
-
substrate specificities of enzyme forms RNase P and RNase MRP
-
-
?
additional information
?
-
-
involved in regulation of noncoding RNA (ncRNA) expression
-
-
?
additional information
?
-
-
yeast RNase P may process antisense RNAs from genes encoding ribosomal proteins
-
-
?
additional information
?
-
-
only a small fraction of the mixed-sequence RNA is cleaved by RNase P. Binding and cleavage of unstructured RNA by nuclear RNase P, overview
-
-
?
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
?
additional information
?
-
-
structures of the acceptor stem and anticodon/intron loop of the tRNA are crucial for Schizosaccharomyces pombe RNase P action
-
-
?
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
?
additional information
?
-
-
assay substrate is tobacco chloroplast precursor tRNAGly
-
-
?
additional information
?
-
-
RNase P enzyme seems to have lost the RNA component during evolution, proving that the catalytic activity of the RNA component of the RNase P holoenzyme can be accomplished by proteins alone
-
-
?
additional information
?
-
-
substitution of a sulfur atom for either the Rp or Sp nonbridging phosphate oxygen or the 3'oxyanion leaving group in pre-tRNA decreases the catalytic rate constant by over 1000fold
-
-
?
additional information
?
-
-
the RNA subunit is the catalytic subunit, while the protein subunits are essential for substrate binding, broad substrate specificity
-
-
?
additional information
?
-
-
cleaves the internal ribosome entry site region in hepatitis C virus RNA near the AUG start codon
-
-
?
additional information
?
-
-
in vitro cleavage of human cytomegalovirus mRNA sequence by M1GS ribozyme. Incubation of a substrate containing the capsid scaffolding protein mRNA sequence with functional ribozyme M1-C1 (3'-terminus of an engineered M1GS ribozyme, V57, covalently linked with a guide sequence of 18 nucleotides that is complementary to the targeted mRNA sequence) yields efficient cleavage. Cleavage of capsid scaffolding protein mRNA by mutant M1-C2 or M1-thymidine kinase is barely detected
-
-
?
additional information
?
-
the enzyme is an RNA-based enzyme primarily catalyzing 5'-end pre-tRNA processing
-
-
?
additional information
?
-
-
the enzyme is an RNA-based enzyme primarily catalyzing 5'-end pre-tRNA processing
-
-
?
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
?
additional information
?
-
-
the enzyme PRORP1 cleaves pre-tRNAs substrates lacking an anticodon arm,n recognition mechanism involves the D-TpsiC loops in tRNA, overview
-
-
?
additional information
?
-
-
essential ribonucleoprotein enzyme responsible for the 5'-end maturation of tRNAs
-
-
?
additional information
?
-
-
RNase P RNA is a substrate of the DEAD box helicase Hera, the specificity of Hera for RNase P RNA may be required for RNase P RNA folding or RNase P assembly
-
-
?
additional information
?
-
-
5'-endonucleolytic precursor tRNA cleavage
-
-
?
additional information
?
-
-
substrate is a RNA-tRNA primary transcript
-
-
?
additional information
?
-
-
the enzyme processes the 5'-end of tRNAs
-
-
?
additional information
?
-
-
substrate used in assays is Escherichia coli pre-tRNATyr
-
-
?
additional information
?
-
-
regulation of gene expression can be achieved by creating a complex made of target mRNA and a complementary small oligonucleotide that resembels natural enzyme substrate
-
-
?
additional information
?
-
-
RNase P is the endonuclease that removes 5' extensions from tRNA precursors
-
-
?
additional information
?
-
-
the natural substrate is precursor tRNA. Proteinaceous PRORP1 catalyzes all of the other noncanonical, yet vital functions of nuclear yeast RNase P, which may include processing of non-canonical RNAs
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
10Sa RNA + H2O
?
-
-
-
-
?
4.55 rRNA precursor + H2O
mature 4.55 rRNA + 5'-oligonucleotide
-
-
-
-
?
4.5S RNA precursor + H2O
mature 4.5S RNA + 5'-oligonucleotide
-
RNA processing
-
-
?
C4 antisense RNA + H2O
?
-
from bacteriophages P1 and P7
-
-
?
polycistronic his operon mRNA precursor + H2O
?
-
-
-
-
?
polycistronic mRNA precursor + H2O
mature mRNAs + ?
-
RNA processing
-
-
?
pre-rRNA + H2O
mature rRNA
pre-tRNA + H2O
?
-
ribonucleoprotein enzyme required for 5'-end maturation of precursor tRNAs (pre-tRNAs)
-
-
?
pre-tRNA + H2O
mature tRNA + 5'-terminal oligonucleotide
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
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
-
-
?
tmRNA precursor + H2O
mature tmRNA + 5'-oligonucleotide
-
RNA processing
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
tRNA precursor + H2O
mature tRNA + 5'-terminal oligonucleotide
tRNA-like pseudoknotted structures in viral RNA + H2O
processed RNA + ?
-
tRNA-like pseudoknotted structures in viral RNA
-
-
?
additional information
?
-
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
mature tRNA + 5'-terminal oligonucleotide
-
-
-
-
?
pre-tRNA + H2O
mature tRNA + 5'-terminal oligonucleotide
-
-
-
-
?
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
-
-
-
-
?
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'-oligoribonucleotide
-
-
-
-
?
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
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
Chlamydomonas reinhardtii cw15 arg7-8 mt+
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
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
-
-
-
-
?
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
the enzyme is involved in maturation of the 5'-end of tRNA
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
-
-
-
?
pre-tRNA + H2O
tRNA + 5'-oligoribonucleotide
-
removal of a 5' leader sequence from tRNA precursor
-
-
?
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
-
-
?
precursor tRNA + H2O
?
-
catalyze the 5' maturation of precursor tRNA
-
-
?
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
?
-
catalyzes the magnesium-dependent 5'-end maturation of tRNAs
-
-
?
ptRNATyr + H2O
?
-
from Escherichia coli
-
-
?
ptRNATyr + H2O
?
-
from Eschericha coli
-
-
?
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, 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, 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, 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
-
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
-
tRNA processing
-
-
?
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, 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, 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
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, maturation
-
-
?
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, maturation, essential
-
-
?
tRNA precursor + H2O
mature tRNA + 5'-oligonucleotide
-
cleavage of 5'-terminal oligonucleotide, maturation, essential
-
-
?
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
-
-
?
additional information
?
-
-
catalyze tRNA 5-end maturation
-
-
?
additional information
?
-
-
5'-endonucleolytic precursor tRNA cleavage
-
-
?
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
?
-
-
other pre-RNAs are also physiological substrates of the enzyme
-
-
?
additional information
?
-
-
substrate specificity is determined by the enzymes' RNA fold, the structure of the specificity domain of the RNA subunit provides the basis of understanding the structurs of other bacterial ribozyme molecules because all bacterial S domains havea common core that comprises stems P7-P11 plus J11/12-J12/11 module, overview
-
-
?
additional information
?
-
-
catalyzes the 5-end maturation of tRNAs in all Kingdoms of life
-
-
?
additional information
?
-
-
5'-endonucleolytic precursor tRNA cleavage
-
-
?
additional information
?
-
-
ribonuclease P catalyzes the metal-dependent 5' end maturation of precursor tRNAs
-
-
?
additional information
?
-
-
the enzyme catalyzes the 5' end maturation of precursor tRNAs (pre-tRNAs)
-
-
?
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
?
additional information
?
-
-
other pre-RNAs are also physiological substrates of the enzyme
-
-
?
additional information
?
-
-
5'-maturation of transfer RNA
-
-
?
additional information
?
-
-
catalyses the 5'-end processing reaction of tRNA precursor molecules
-
-
?
additional information
?
-
-
essential ribonucleoprotein enzyme responsible for the 5'-end maturation of tRNAs
-
-
?
additional information
?
-
-
5'-endonucleolytic precursor tRNA cleavage
-
-
?
additional information
?
-
-
precursor tRNAs are natural enzyme RNase P substrates
-
-
?
additional information
?
-
-
the enzyme processes the 5' ends of tRNA precursors, the substrate population includes over 80 different competing ptRNAs in Escherichia coli, sequence and secondary structure of representative ptRNAs, overview. Its mode of molecular recognition differs from other catalytic RNAs in two important ways. First, its biological role in ptRNA processing requires that it act in trans as a multiple turnover enzyme, whereas other ribozymes, with the exceptions of the ribosome and spliceosome, undergo single turnover self-splicing or self-cleavage reactions. Second, RNase P processes multiple RNA substrates, including all ptRNAs in the cell, whereas other ribozymes, again with the exceptions of the ribosome and spliceosome, have one specific substrate
-
-
?
additional information
?
-
-
the mechanism by which the enzyme processes the valU and lysT polycistronic transcripts (valV valW, valU valX, valY lysY and lysT valT lysW valZ lysY lysZ lysQ) involves initiation of processing by first endonucleolytically removing the Rho-independent transcription terminators from the primary valU and lysT transcripts. Subsequently, the enzyme proceeds in the 3' -> 5' direction generating one pre-tRNA at a time. Identification of cleavage sites using RNA circularization, overview
-
-
?
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
?
additional information
?
-
-
the mechanism by which the enzyme processes the valU and lysT polycistronic transcripts (valV valW, valU valX, valY lysY and lysT valT lysW valZ lysY lysZ lysQ) involves initiation of processing by first endonucleolytically removing the Rho-independent transcription terminators from the primary valU and lysT transcripts. Subsequently, the enzyme proceeds in the 3' -> 5' direction generating one pre-tRNA at a time. Identification of cleavage sites using RNA circularization, overview
-
-
?
additional information
?
-
-
biosynthesis and regulation of RNase P, transient interactions with several proteins in the cell, the protein subunits are conserved between RNase P and RNase MRP, and are essential for cell viability and enzyme function, overview, enzyme subunits in nucleolus and Cajal bodies might be involved in cell mitosis and cell-cycle-dependent gene transcription
-
-
?
additional information
?
-
-
coordination of RNA pathways, overview
-
-
?
additional information
?
-
-
the human mitochondrial RNase P is an entirely protein-based enzyme, protein MRPP1, a probable tRNA methylase, provides tRNA-binding specificity to the RNase P enzyme, protein MRPP2 binds tightly to MRPP1 and is a member of the short chain dehydrogenase/reductase protein family, protein MRPP3 may provide the enzymatic cleavage activity for the patchwork enzyme
-
-
?
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
?
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
?
additional information
?
-
-
phylogenetic study of archeal enzymes
-
-
?
additional information
?
-
-
5-maturation of transfer RNA
-
-
?
additional information
?
-
-
phylogenetic study of archeal enzymes
-
-
?
additional information
?
-
-
5-maturation of transfer RNA
-
-
?
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
?
additional information
?
-
-
essential ribonucleoprotein enzyme responsible for the 5'-end maturation of tRNAs
-
-
?
additional information
?
-
-
5-maturation of transfer RNA
-
-
?
additional information
?
-
-
the enzyme is a ribonuleoprotein that catalyzes the processing of 5' leader sequences from tRNA precursors and other noncoding RNA
-
-
?
additional information
?
-
-
coordination of RNA pathways, overview
-
-
?
additional information
?
-
-
the mitochondrial ribozyme RNA subunit might have a cellular function outside the mitochondria
-
-
?
additional information
?
-
-
transient interactions with several proteins in the cell, e.g. protein subunit Rpp20 interacts with the heat shock protein Hsp27, protein subunit Rpp14 interacts with several proteins including the LIM domain protein 1 LIMD1 and the SR-rich HSPC232
-
-
?
additional information
?
-
-
involved in regulation of noncoding RNA (ncRNA) expression
-
-
?
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
?
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
?
additional information
?
-
the enzyme is an RNA-based enzyme primarily catalyzing 5'-end pre-tRNA processing
-
-
?
additional information
?
-
-
the enzyme is an RNA-based enzyme primarily catalyzing 5'-end pre-tRNA processing
-
-
?
additional information
?
-
-
the natural substrate is precursor tRNA
-
-
?
additional information
?
-
-
essential ribonucleoprotein enzyme responsible for the 5'-end maturation of tRNAs
-
-
?
additional information
?
-
-
5'-endonucleolytic precursor tRNA cleavage
-
-
?
additional information
?
-
-
the enzyme processes the 5'-end of tRNAs
-
-
?
additional information
?
-
-
regulation of gene expression can be achieved by creating a complex made of target mRNA and a complementary small oligonucleotide that resembels natural enzyme substrate
-
-
?
additional information
?
-
-
RNase P is the endonuclease that removes 5' extensions from tRNA precursors
-
-
?
additional information
?
-
-
the natural substrate is precursor tRNA. Proteinaceous PRORP1 catalyzes all of the other noncanonical, yet vital functions of nuclear yeast RNase P, which may include processing of non-canonical RNAs
-
-
?
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Li+
-
less effective in activation than K+
MgCl2
-
optimal activity at 5 mM
Pb2+
-
Pb2+ can replace Mg2+
Sr2+
-
Mg2+, Ca2+, Sr2+, and, to a lesser extent, Mn2+ can perform the electrostatic shielding function and preserve the structural properties of the two RNA molecules necessary to keep the substrate and enzyme in appropriate conformations
Ca2+
-
much less efficiently than Mg2+ or Mn2+
Ca2+
-
suppresses enzyme activity, but supports RNA folding and substrate binding, used for binding assays
Ca2+
-
presence of the protein cofactor increases and equalizes substrate affinity and abolishes the substrate affinity differences seen for Escherichia coli relative to Bacillus subtilis P RNA
Ca2+
-
stabilizes RNase P folding and substrate binding with little activation of catalytic activity. Affinity of RNase P for A(-4) pre-tRNA increases 4fold as the Ca2+ concentration increases from 2 mM to 5 mM. Affinity for the G(-4) substrate increases 65fold over the same range
Ca2+
-
time courses for fluorescein-labeled pre-tRNA binding to RNase P are biphasic in the presence of both Ca2+ and Mg2+II, requiring a minimal two-step association mechanism. With Ca2+, pre-tRNA cleavage is slow
Ca2+
-
a divalent cation stabilizes the active conformation of the RNase P-pre-tRNA complex, a role for an inner-sphere metal ion, Mg2+ or Ca2+, in the enzyme. Structural changes that occur upon binding Ca(II) to the ES complex are determined by time-resolved FRET measurements of the distances between donor/acceptor fluorophores introduced at specific locations on the P protein and pre-tRNA 5' leader. The value of KD,obs has an apparent hyperbolic dependence on the concentration of calcium with an apparent dissociation constant for Ca(II) of 0.04 mM
Ca2+
-
metal-stabilized conformational change in RNase P that accompanies substrate binding and is essential for efficient catalysis
Ca2+
-
Mg2+, Ca2+, Sr2+, and, to a lesser extent, Mn2+ can perform the electrostatic shielding function and preserve the structural properties of the two RNA molecules necessary to keep the substrate and enzyme in appropriate conformations
Ca2+
-
presence of the protein cofactor increases and equalized substrate affinity and abolishes the substrate affinity differences seen for Escherichia coli relative to Bacillus subtilis P RNA
Ca2+
-
Ca2+ can replace Mg2+
Cd2+
-
changes the cleavage pattern
Cd2+
-
changes the cleavage pattern
Cs+
-
less effective in activation than K+
Cs+
-
supports activity at 100-200 mM
Cu2+
-
changes the cleavage pattern
Cu2+
-
changes the cleavage pattern
K+
-
optimal concentration 40-60 mM
K+
-
optimal activity at 0.3-1 M NH4Cl or KCl
K+
-
optimal activity in presence of 5 mM KCl or 10 mM NH4Cl
K+
-
monovalent cation required, K+ is most effective
K+
-
monovalent cation required: Na+, K+ or NH4+
K+
-
stimulates at less than 30 mM
K+
-
optimal activity at 150-200 mM KCl
K+
-
maximal activity at 0.1-0.2 M
KCl
-
activates, best at 200 mM
KCl
-
optimal concentration: 200 mM
Mg2+
-
-
Mg2+
activates, the enzyme requires at least two Mg2+ ions for optimal catalysis. Mg2+ ions bind cooperatively to PRORP1
Mg2+
-
10-15 mM required for optimal activity
Mg2+
-
optimal concentration: 60-90 mM
Mg2+
-
optimal activity at 20-200 mM MgCl2
Mg2+
-
strict requirement for a divalent cation, Mg2+ or Mn2+. Hexacoordinated Mg2+ binds to the catalytic site on M1 RNA
Mg2+
-
required for catalysis
Mg2+
-
absolutely required, optimal at about 20 mM, for catalysis and substrate shape recognition, influences substrate binding affinity
Mg2+
-
best metal ion, required for folding of the RNA, for binding of protein and substrate, and for catalytic activity
Mg2+
-
interaction with the helix P4
Mg2+
-
potential catalytic transition state structure including 3 required divalent metal ions, coordinated to nonbinding phosphate group oxygens
Mg2+
-
preferred metal ion, absolutely required
Mg2+
-
enzymatic activity depends on the presence of divalent metal ions such as Mg2+
Mg2+
-
60 mM is optimal for the holoenzyme
Mg2+
-
significant association of Mg2+ ions at the P4 major groove of RNase P near the flexible pivot point (A5, G22, and G23)
Mg2+
-
time courses for fluorescein-labeled pre-tRNA binding to RNase P are biphasic in the presence of both Ca2+ and Mg2+II, requiring a minimal two-step association mechanism. Cleavage rate constants are significantly higher in the presence of the physiologically important metal cofactor magnesium
Mg2+
-
a divalent cation stabilizes the active conformation of the RNase P-pre-tRNA complex, a role for an inner-sphere metal ion, Mg2+ or Ca2+, in the enzyme. A second, lower affinity Mg(II) activates cleavage catalyzed by the enzyme
Mg2+
-
metal-stabilized conformational change in RNase P that accompanies substrate binding and is essential for efficient catalysis
Mg2+
-
enzymatic activity depends on the presence of divalent metal ions such as Mg2+
Mg2+
-
the RNA subunit requires 20 mM Mg2+ for optimal activity
Mg2+
-
preferred metal ion, absolutely required
Mg2+
-
optimal activity in presence of 5 mM MgCl2
Mg2+
-
required for activity
Mg2+
-
required for activation
Mg2+
-
the only metal ion that can act as cofactor for activity of M1 RNA
Mg2+
-
Mg2+, Ca2+, Sr2+, and, to a lesser extent, Mn2+ can perform the electrostatic shielding function and preserve the structural properties of the two RNA molecules necessary to keep the substrate and enzyme in appropriate conformations
Mg2+
-
can substitute for the C5 protein as a cofactor, since M1 RNA alone can carry out the catalytic reaction in the buffer that contains more than 20 mM Mg2+
Mg2+
-
strict requirement for a divalent cation, Mg2+ or Mn2+. Hexacoordinated Mg2+ binds to the catalytic site on M1 RNA
Mg2+
-
required for efficient cleavage at the correct position. Essential for the folding of the active conformation of RNase P RNA
Mg2+
-
absolutely required, optimal at about 10 mM, for catalysis and substrate shape recognition, influences substrate binding affinity
Mg2+
-
best metal ion, required for folding of the RNA, for binding of protein and substrate, and for catalytic activity
Mg2+
-
coordination to nucleotide A67 of the enzymes RNA
Mg2+
-
interaction with the helix P4
Mg2+
-
potential catalytic transition state structure including 3 required divalent metal ions, coordinated to nonbinding phosphate group oxygens
Mg2+
-
preferred metal ion, absolutely required
Mg2+
-
required for hyperprocessing reaction, at about 10 mM
Mg2+
-
replacement, deletion, or insertion (except at G63G64) of bases of the J3/4 domain of Escherichia coli ribonuclease P, can be compensated for by the presence of a high concentration of magnesium ions above 20 mM
Mg2+
-
essential for activity, the ribozyme prefers the wild type pre-tRNA (A7) substrate at low Mg2+
Mg2+
-
10 mM is optimal for the holoenzyme
Mg2+
-
for the LNA variant, parallel pathways leading to cleavage at the c0 and m+1 sites have different pH profiles, with a higher Mg2+ requirement for c0 versus m+1 cleavage. The strong catalytic defect for LNA and 2'-OCH3 supports a model where the extra methylene (LNA) or methyl group (2'-OCH3) causes a steric interference with a nearby bound catalytic Mg2+ during its recoordination on the way to the transition state for cleavage. Presence of the protein cofactor suppresses the ground state binding defects, but not the catalytic defects
Mg2+
-
required, the requirement of Mg2+ for catalysis varies with the substrate. Deletion of the S-domain changes the Mg2+ requirement
Mg2+
-
required for folding, substrate binding, and catalysis
Mg2+
-
optimal concentration is 55 mM
Mg2+
-
optimal activity at 5 mM
Mg2+
-
is the most effective cofactor, can be replaced by Mn2+
Mg2+
-
preferred metal ion, absolutely required
Mg2+
-
required, optimal cleavage at 20 mM for the reconstituted mini-enzyme, reduced activity at 40-100 mM, the wild-type enzyme shows no activity at 100 mM
Mg2+
-
dependent on, the optimum is at 5 mM MgCl2, when reactions are carried out at pH 7.5 and 37°C
Mg2+
-
enzymatic activity depends on the presence of divalent metal ions such as Mg2+
Mg2+
-
mitochondrial RNase P requires divalent metal ions, preferably Mg2+, for cleavage
Mg2+
-
maximally active at 2.5-30 mM MgCl2
Mg2+
-
dependent on, optimal at 2-10 mM
Mg2+
-
dependent on, at least half-maximal activity between 8-80 mM
Mg2+
-
preferred metal ion, absolutely required
Mg2+
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)
Mg2+
-
optimal concentration for RNase P RNA activity is 250 mM MgCl2
Mg2+
-
optimal 120 mM RNase P RNA + RNase P protein 21 + RNase P protein 29
Mg2+
-
required for activation
Mg2+
-
the bulge stem-loop structure containing J3/4 and helix P4 is involved in the interaction with Mg2+ ions important for catalysis
Mg2+
-
optimal activity at 1 mM MgCl2
Mg2+
-
optimally at 7.5 mM
Mg2+
-
dependent on, binds to the pro-Rp nonbridging oxygen of the scissile bond, coordination
Mg2+
-
high activation, specific for
Mg2+
-
preferred metal ion, absolutely required
Mg2+
-
required for formation of the Pop6-Pop7-RNA complex
Mg2+
-
strict requirement for a divalent cation, Mg2+ or Mn2+. Hexacoordinated Mg2+ binds to the catalytic site on M1 RNA
Mg2+
-
required at a concentration of at least 2 mM
Mg2+
-
best metal ion, required for folding of the RNA, for binding of protein and substrate, and for catalytic activity
Mg2+
-
optimal at 5-10 mM for the holoenzyme, the RNA subunit alone is active only at 100 mM MgCl2
Mg2+
required, the active site includes at least two metal ions, RNA U52 nucleotide binds a metal ion at the active site
Mn2+
-
-
Mn2+
activates, two manganese ions are bound to the active site interacting with four conserved aspartate residues (D399A, D474A, D475A, and D493A) through both inner and outer sphere interactions
Mn2+
-
strict requirement for a divalent cation, Mg2+ or Mn2+
Mn2+
-
can substitute for Mg2+, slightly lower activity
Mn2+
-
substitution of Mg2+ by Mn2+ can result in miscleavage of the substrate containing a N(-1)/N(73) pair, better sulfur coordination compared to Mg2+
Mn2+
-
Mn2+ paramagnetic line broadening experiments reveal strong metal localization at residues corresponding to G378 and G379
Mn2+
-
can substitute for Mg2+, slightly lower activity
Mn2+
-
effectively substitutes for Mg2+
Mn2+
-
Mg2+, Ca2+, Sr2+, and, to a lesser extent, Mn2+ can perform the electrostatic shielding function and preserve the structural properties of the two RNA molecules necessary to keep the substrate and enzyme in appropriate conformations
Mn2+
-
can promote catalysis
Mn2+
-
strict requirement for a divalent cation, Mg2+ or Mn2+
Mn2+
-
rescues A67Rp- and A67Sp-phosphorothionate modified inactive enzyme at 5 mM completely and partially, respectively
Mn2+
-
substitution of Mg2+ by Mn2+ can result in miscleavage of the substrate containing a N(-1)/N(73) pair, better sulfur coordination compared to Mg2+
Mn2+
-
Mn2+ can replace for Mg2+ in activation
Mn2+
-
Mn2+ can replace Mg2+
Mn2+
-
can substitute for Mg2+, slightly lower activity
Mn2+
-
can substitute for Mg2+, slightly lower activity
Mn2+
-
strict requirement for a divalent cation, Mg2+ or Mn2+
Na+
-
less effective in activation than K+
Na+
-
monovalent cation required: Na+, K+ or NH4+
Na+
-
less effective in activation than K+
Na+
-
supports activity at 100-200 mM
NaCl
-
activates
NaCl
-
optimal concentration: 50 mM
NaCl
-
activates, best at 50 mM
NH4+
-
optimal concentration: 40-60 mM
NH4+
-
optimal concentration: 100-200 mM
NH4+
-
optimal activity at 0.3-1 M NH4Cl or KCl
NH4+
-
800 mM NH4Cl is required for optimal activity. (NH4)2SO4 is significantly more active than NH4Cl
NH4+
-
optimal activity in presence of 5 mM KCl or 10 mM NH4Cl
NH4+
-
stimulates activity of M1 RNA
NH4+
-
monovalent cation required, NH4+ is less effective than K+
NH4+
-
monovalent cation required: Na+, K+ or NH4+. Optimal NH4+ concentration is 200 mM
NH4+
-
dependent on, the optimum is at 70 mM NH4Cl, when reactions are carried out at pH 7.5 and 37°C
NH4+
-
optimal concentration for RNase P RNA activity is 3 M NH4Cl
NH4+
-
supports activity at 300 mM
NH4Cl
-
activates, best at 200-400 mM
NH4Cl
-
optimal concentration: 200-400 mM
Ni2+
activates
Ni2+
-
changes the cleavage pattern
Ni2+
-
changes the cleavage pattern
Zn2+
bound by conserved residues. A putative zinc-finger-like structure is split in two separate motifs. The first motif (CxxC) contains two conserved cysteines upstream of the NYN domain at positions 344 and 347 for PRORP1, whereas the second motif involves a conserved histidine and a cysteine, downstream of the NYN domain, at positions 548 and 565, respectively. The downstream conserved motif has a stronger affinity for the metal than the upstream CxxC coordination element
Zn2+
-
Zn2+ is involved in inner-sphere interactions with the P4 helix mimic of RNase P, the bound Zn2+ exhibits six-coordinate geometry with an average Zn2+-O/N bond distance of 2.08 A
Zn2+
-
Zn2+ can replace Mg2+
additional information
-
divalent metal cations are essential
additional information
-
divalent metal cations are essential for catalysis and stabilize the enzyme conformation and subunit interaction
additional information
-
divalent metal ions are absolutely required, reduced activity with Ca2+
additional information
-
divalent metal ions are important cofactors for the catalytic reaction and for substrate binding at the conserved loops CR-II and CR-III in proximity to the substrate aminoacyl stem, enhancement of substrate affinity by 1000fold
additional information
-
enzyme is dependent on divalent metal ions, enzyme contains a metal binding loop
additional information
-
catalysis of pre-tRNA cleavage by RNase P requires at least one divalent cation capable of forming inner-sphere coordination, such as Mg2+, Mn2+, Zn2+ or Ca2+
additional information
-
divalent metal ions are absolutely required, reduced activity with Ca2+
additional information
-
divalent metal cations are essential
additional information
-
divalent metal ions are important cofactors for the reaction
additional information
-
requires a monovalent and a divalent cation for activity
additional information
-
at least 2 metal ions per enzyme molecule, one catalytically and one structurally important, interactions of divalent metal cations at the pro-Rp and ProSp non-bridging phosphate oxygens with nucleotide A67 in the universally conserved helix p4 are essential for the folding and function of the enzymes' catalytic RNA component, interaction kinetics
additional information
-
divalent metal cations are essential
additional information
-
divalent metal cations are essential for catalysis and stabilize the enzyme conformation and subunit interaction
additional information
-
divalent metal ions are important cofactors for the catalytic reaction and for substrate binding at the conserved loops CR-II and CR-III in proximity to the substrate aminoacyl stem
additional information
-
enzyme is dependent on divalent metal ions
additional information
-
Mn2+, Co2+, Ni2+, Cu2+, Au3+, Pb2+, La3+, Pr3+, Sm3+, Gd3+, Dy3+, Yb3+, and Lu3+ are able to bind to RNase P but are not specific proxies for Mg2+
additional information
-
Ca2+ and Mn2+ cannot substitute for Mg2+
additional information
-
divalent metal cations are essential
additional information
-
divalent metal ions are absolutely required, reduced activity with Ca2+
additional information
-
divalent metal ions are important cofactors for the reaction
additional information
-
divalent metal cations are essential
additional information
-
optimal ionic strength at 800 mM ammonium acetate at 60°C
additional information
-
at least half-maximal activity at 1 M ammonium acetate
additional information
-
divalent metal ions are important cofactors for the reaction
additional information
-
divalent metal cations are essential
additional information
-
requires a monovalent and a divalent cation for activity
additional information
-
divalent metal ions are absolutely required, reduced activity with Ca2+
additional information
-
divalent metal ions are important cofactors for the reaction
additional information
-
Mg2+ is not required for activity
additional information
-
enzyme is dependent on divalent metal ions, enzyme contains a metal binding loop
additional information
-
divalent metal cations are essential
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metabolism
the enzyme is involved in maturation of the 5'-end of tRNA
evolution
comparison of nuclear, mitochondrial, and plastidic RPPs, overview
evolution
-
Dictyostelium discoideum nuclear RNase P is a ribonucleoprotein complex that displays similarities with its counterparts from higher eukaryotes such as the human enzyme, but at the same time it retains distinctive characteristics
evolution
-
evolutionary history of PRORP, overview
evolution
-
identification in select archaea of an unusual archetype of the RNase P RNA
evolution
-
the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs
evolution
-
the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs
evolution
-
the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs
evolution
-
the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs
evolution
-
the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs
evolution
-
the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs
evolution
-
the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs
evolution
-
the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs
evolution
-
the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs
evolution
-
in the evolved, modern RNase P enzymes, the RNA depends on protein to fulfill its cellular function. This RNA-based form of RNase P is found in all domains of life, but there is an apparent trend from RNA to protein predominance in the overall composition and functioning of these ribonucleoproteins from bacteria to eukarya. RNase P of the former is built from a catalytically proficient RNA and a single small protein only. RNase P RNA of Archaea is a less-efficient catalyst in vitro and associates with five proteins, none of which is related to the bacterial protein. Another entirely different form of RNase P, i.e. proteinaceous RNase P, apparently not containing RNA, is initially observed in the organelles of different eukarya, e.g. humans, and also in Trypanosoma brucei. The genomes of trypanosomatids lack evidence for genes related to RNA-based RNase P, but they encode two homologues of human and plant PRORP genes. Also in plants, all cellular tRNA 5' end maturation appears to be exclusively protein dependent
evolution
-
the enzyme is conserved in all domains of life. The composition of RNase P varies from bacteria to archaea and eukarya, evolutionary enzyme spread, overview
evolution
-
the enzyme is conserved in all domains of life. The composition of RNase P varies from bacteria to archaea and eukarya, evolutionary enzyme spread, overview
evolution
-
the enzyme is conserved in all domains of life. The composition of RNase P varies from bacteria to archaea and eukarya, evolutionary enzyme spread, overview
evolution
-
the enzyme is conserved in all domains of life. The composition of RNase P varies from bacteria to archaea and eukarya, evolutionary enzyme spread, overview
evolution
the enzyme is conserved in all domains of life. The composition of RNase P varies from bacteria to archaea and eukarya, evolutionary enzyme spread, overview
evolution
-
the enzyme is conserved in all domains of life. The composition of RNase P varies from bacteria to archaea and eukarya, evolutionary enzyme spread, overview. The chloroplast and mitochondrial genomes of Ostreococcus tauri encode distinct individual RNase P RNA genes and the nucleus encodes both a bacterial-like RNase P protein component, and a proteinaceous RNase P enzyme
evolution
-
the enzyme is conserved in all domains of life. The composition of RNase P varies from bacteria to archaea and eukarya, evolutionary enzyme spread, overview. The protozoan Trypanosoma brucei harbors 2 PRORP isoforms, both of which have 5' pre-tRNA processing activity in vitro. One isoform (PRORP1) localizes to the nucleus and the second (PRORP2) to the mitochondrion
evolution
-
two architectural subtypes of bacterial P RNAs, the phylogenetically prevailing ancestral type A represented by Escherichia coli P RNA, and Bacillus type B essentially confined to the low G + C Gram-positive bacteria, the prototype being Bacillus subtilis P RNA
evolution
-
two architectural subtypes of bacterial P RNAs, the phylogenetically prevailing ancestral type A represented by Escherichia coli P RNA, and Bacillus type B essentially confined to the low G + C Gram-positive bacteria, the prototype being Bacillus subtilis P RNA
evolution
-
Yeast RNase P has lost RNA elements that serve as structural braces in its bacterial and, by inference, archaeal counterparts, but has gained proteins Pop1, Pop6, Pop7 and Pop8 that are not found in archaea
evolution
-
comparison of nuclear, mitochondrial, and plastidic RPPs, overview
-
evolution
-
Dictyostelium discoideum nuclear RNase P is a ribonucleoprotein complex that displays similarities with its counterparts from higher eukaryotes such as the human enzyme, but at the same time it retains distinctive characteristics
-
malfunction
-
genetic alterations in either the RNA or protein subunit impair enzyme activity in vitro. A structural mutation in the RNase P protein (temperature-sensitive mutant ts241) affects the RNase P RNA level in vivo
malfunction
-
in a strain carrying the rnpA49 allele, encoding temperature sensitive RNase P, thermal inactivation of RNase P leads to ca. 60% reduction in relative quantities of the mature tRNA, although there is no change the relative quantities of the primary transcripts. Inactivation of both RNase P and RNase E leads to disappearance of the majority of the heterogeneous pre-tRNA precursor species except for the species containing the intact 5'-end and a processed 3'-end. In the absence of RNase P (both rnpA49 and rnpA49 rne-1) ca. 77% (36/49) of the transcripts have immature 3' termini containing 1-3 nt downstream of the CCA
malfunction
-
in both deletion mutants Rpp20(16-140) and Rpp20(35-140) the global thermodynamics of the interaction with Rpp25 is seemingly unaffected. Thermodynamic signature of the association is also fully preserved between the Rpp25(25-170) mutant and all available versions of Rpp20. Regions within the mutants Rpp20(35-140) and Rpp25(25-170) are sufficient for mutual interaction, thus this recognition can be mediated largely, if not exclusively, by the Alba-type core domains
malfunction
-
inactivation of RNase P results in decreased transcription of several non-coding RNAs in a cell cycle-dependent fashion
malfunction
-
mutant M1-C2 is catalytically inactive
malfunction
-
absence of the enzyme in mutant rnpA49 rph-1 strain results in accumulation of unprocessed large tRNA transcripts and a 4fold decrease in mature species
malfunction
-
deletion of the S-domain reduces the activity rate, changes the Mg2+ requirement, and has a significant impact on the kinetic of cleavage for substrates carrying C-1/G+73. Substitutions in the truncated mutant, e.g. at pposition 248, can partly compensate for the absence of the S-domain, overview
malfunction
-
mutations in the RNR motif of P protein alter the affinity of PRNA for P protein, and of RNase P for pre-tRNAAsp, overview
malfunction
-
downregulation results in impaired tRNA biogenesis in both organelles and the nucleus
malfunction
in both plastids and mitochondria, the effects of PRORP1 knock-down on the processing of individual tRNA species are highly variable. While a few tRNAs are severely affected, many others show little or no changes in accumulation of the mature tRNA. The drastic reduction in the levels of mature plastid tRNA-Phe(GAA) and tRNA-Arg(ACG) suggests that these two tRNA species limit plastid gene expression in the PRORP1 mutants and, hence, are causally responsible for the mutant phenotype
malfunction
Chlamydomonas reinhardtii cw15 arg7-8 mt+
-
downregulation results in impaired tRNA biogenesis in both organelles and the nucleus
-
malfunction
-
in a strain carrying the rnpA49 allele, encoding temperature sensitive RNase P, thermal inactivation of RNase P leads to ca. 60% reduction in relative quantities of the mature tRNA, although there is no change the relative quantities of the primary transcripts. Inactivation of both RNase P and RNase E leads to disappearance of the majority of the heterogeneous pre-tRNA precursor species except for the species containing the intact 5'-end and a processed 3'-end. In the absence of RNase P (both rnpA49 and rnpA49 rne-1) ca. 77% (36/49) of the transcripts have immature 3' termini containing 1-3 nt downstream of the CCA
-
malfunction
-
absence of the enzyme in mutant rnpA49 rph-1 strain results in accumulation of unprocessed large tRNA transcripts and a 4fold decrease in mature species
-
physiological function
-
an in vitro transcribed RNase P RNA is catalytically active
physiological function
-
assembly of the mature RNase P RNA with its cognate protein subunit ensures longevity of the holoenzyme complex in vivo. Increased growth rate of the organism coincides with increased RNase P RNA copy number
physiological function
-
binding of RPP29 to RPP21 involves binding-coupled folding and stabilization of interfacial structures in RPP29. When bound to its partner, RPP21 adopts the same overall L-shaped structure observed in the free protein: a long arm containing the two N-terminal alpha-helices, a short-arm made up of the C-terminal beta-sheet comprising the zinc ribbon, and a central linker connecting the two domains. In the complex, helix alpha1 of RPP21 extends through residues 9-17, indicating that binding is associated with induced fit in RPP21 as well. The N-terminal region of RPP29 extends in an antiparallel fashion along RPP21 helix alpha1. RPP29 beta2 interacts with both helices of RPP21 in the center of the interface, and the C-terminal helix of RPP29 stabilizes the end of RPP21 helix alpha2. The RPP21RPP29 complex is localized to the specificity domain of the RNase P RNA. Sm-like core of RPP29 is essentially unchanged by RPP21 binding
physiological function
-
Ignicoccus hospitalis is the host of Nanoarchaeum equitans, who has no RNase P and is dependent on its host RNase P activity for transfer of metabolites, energy and amino acids
physiological function
-
in the presence of the RPP29RPP21 complex, the paired regions P9, P10/11, and P12 in the S-domain are protected from V1 cleavage, while no protection by RPP29RPP21 complex is observed in the C-domain
physiological function
-
mitochondrial RNase P RNA is primitive and recognizably similar to those of alpha-proteobacteria, the ancestors of mitochondria
physiological function
-
native nuclear RNase P has an RNase P RNA plus nine RNase P proteins. All subunits are essential for RNase P activity and cell viability. Only the nuclear-encoded RPM2 is known and shown genetically to be required for mitochondrial RNase P activity
physiological function
-
native nuclear RNase P has an RNase P RNA plus ten RNase P proteins. The protein-only mitochondrial RNase P is composed of three proteins (MRPP1-MRPP3). MRPP1, which methylates G9 of tRNAs, may be responsible for substrate recognition. RNase P RNA is weakly active without RNase P proteins, some activity is present when reconstituted with RPP21 and RPP29
physiological function
-
plastid RNase P RNA in the non-green alga is similar to those of their cyanobacterial ancestry
physiological function
-
RNase P is an essential enzyme that catalyzes the 5' endonucleolytic cleavage of pre-tRNAs. RNase MRP, a variant of RNase P that has evolved to participate in ribosomal RNA processing, is also involved in turnover of specific messenger RNAs. RNase P and RNase MRP have eight proteins in common, with the RNA subunits being related but diverged. RNase P has one distinctive protein subunit (Rpr2p), while RNase MRP has two (Snm1p, Rmp1p). Nuclear RNase P is involved in a pathway for alternative maturation of intron-encoded box C/D snoRNAs
physiological function
-
RNase P is required in all free-living cells, RNase P is encoded even in the most compact bacterial genome of Mycoplasma genitalium
physiological function
-
Salmonella can efficiently deliver RNase P-based ribozyme sequence in specific human cells, leading to substantial ribozyme expression and effective inhibition of viral infection: targeted gene delivery of RNase P ribozyme by Salmonella to human cytomegalovirus-infected cells results in effective inhibition of viral gene expression and replication. Functional RNase P ribozyme (M1GS RNA) that targets the overlapping mRNA region of two human cytomegalovirus capsid proteins, the capsid scaffolding protein and assemblin, which are essential for viral capsid formation. A reduction of 87-90% in viral capsid scaffolding protein expression and a reduction of about 5000fold in viral growth in cells that are treated with Salmonella carrying the sequence of the functional ribozyme
physiological function
-
strong interaction between Rpp25 and Rpp20. Rpp20 and Rpp25 interact with the P3 arm of RNase MRP RNA in a highly synergic fashion. Rpp20 and Rpp25 interact with the P3 RNA as a heterodimer, which is formed prior to RNA binding. Association between Rpp20 and Rpp25 has no detectable influence on their secondary/tertiary structure. The association reaction results in a large loss of solvent-accessible area. N- and C-terminal regions of Rpp25 and the N-terminal tail of Rpp20 are not involved in mutual recognition
physiological function
-
the holoenzyme consists of a single RNase P RNA associated with RNase P protein subunits
physiological function
-
the mitochondrial RNase P is devoid of any RNA, mitochondria make their RNase P of three proteins only. MRPP1 is involved in the methylation of G9 in mitochondria in addition to its role in mitochondrial RNase P. MRRP2 may contribute RNA binding activity to mitochondrial RNase P via its conserved NAD+-binding domain. In its C-terminal half MRPP3 displays a handful of amino acid residues strictly conserved in their identity and spacing and reminiscent of a metallonuclease's active site: three aspartates and a histidine, the latter proposed to be directly involved in catalysis
physiological function
-
the nuclear holoenzyme is comprised of protein subunits and RNase P RNA. In mitochondria, the usual RNA-containing RNase P is replaced by an enzyme composed of three proteins that are unrelated to RNase P enzymes in other systems (Rube Goldberg triad of unrelated proteins), but nevertheless are together responsible for the cleavage of pre-tRNA precursors
physiological function
-
the organism has distinct RNase P enzymes in the nucleus and mitochondria. The RNase P RNA from the mitochondrion is an example of a highly-derived (degenerate) mitochondrial RNase P RNA
physiological function
-
the RNase P holoenzyme is composed of a single RNA (type A1 RNase P RNA) and a single small protein subunit. Bacterial RNase P RNAs are comprised of two independently evolving domains, separated by P7. The RNA upstream and downstream of P7 contains all of the essential catalytic sequences and structures (C-domain). Changes in the RNA bound at each end by the two strands of P7 (the loop of P7) alter substrate specificity (S-domain). The RNA subunit is associated with a single, small conservative protein, encoded by the rnpA gene, which has an unusual left-handed betaalphabeta crossover connection and a large central cleft
physiological function
-
the RNase P holoenzyme is composed of a single RNA (type A2 RNase P RNA, lacks P13 and P14) and a single small protein subunit. Bacterial RNase P RNAs are comprised of two independently evolving domains, separated by P7. The RNA upstream and downstream of P7 contains all of the essential catalytic sequences and structures (C-domain). Changes in the RNA bound at each end by the two strands of P7 (the loop of P7) alter substrate specificity (S-domain). The RNA subunit is associated with a single, small conservative protein, encoded by the rnpA gene, which has an unusual left-handed betaalphabeta crossover connection and a large central cleft
physiological function
-
the RNase P holoenzyme is composed of a single RNA (type A3 RNase P RNA, with an altered L15 internal loop, in which the substrate 3'-NCCA tail is recognized) and a single small protein subunit. Bacterial RNase P RNAs are comprised of two independently evolving domains, separated by P7. The RNA upstream and downstream of P7 contains all of the essential catalytic sequences and structures (C-domain). Changes in the RNA bound at each end by the two strands of P7 (the loop of P7) alter substrate specificity (S-domain). The RNA subunit is associated with a single, small conservative protein, encoded by the rnpA gene, which has an unusual left-handed betaalphabeta crossover connection and a large central cleft
physiological function
-
the RNase P holoenzyme is composed of a single RNA (type A4 RNase P RNA, with an altered L15) and a single small protein subunit. Bacterial RNase P RNAs are comprised of two independently evolving domains, separated by P7. The RNA upstream and downstream of P7 contains all of the essential catalytic sequences and structures (C-domain). Changes in the RNA bound at each end by the two strands of P7 (the loop of P7) alter substrate specificity (S-domain). The RNA subunit is associated with a single, small conservative protein, encoded by the rnpA gene, which has an unusual left-handed betaalphabeta crossover connection and a large central cleft
physiological function
-
the RNase P holoenzyme is composed of a single RNA (type A5 RNase P RNA, lacks P18) and a single small protein subunit. Bacterial RNase P RNAs are comprised of two independently evolving domains, separated by P7. The RNA upstream and downstream of P7 contains all of the essential catalytic sequences and structures (C-domain). Changes in the RNA bound at each end by the two strands of P7 (the loop of P7) alter substrate specificity (S-domain). The RNA subunit is associated with a single, small conservative protein, encoded by the rnpA gene, which has an unusual left-handed betaalphabeta crossover connection and a large central cleft
physiological function
-
the RNase P holoenzyme is composed of a single RNA (type B1 RNase P RNA) and a single small protein subunit. Bacterial RNase P RNAs are comprised of two independently evolving domains, separated by P7. The RNA upstream and downstream of P7 contains all of the essential catalytic sequences and structures (C-domain). Changes in the RNA bound at each end by the two strands of P7 (the loop of P7) alter substrate specificity (S-domain). The RNA subunit is associated with a single, small conservative protein, encoded by the rnpA gene, which has an unusual left-handed betaalphabeta crossover connection and a large central cleft
physiological function
-
the RNase P holoenzyme is composed of a single RNA (type B2 RNase P RNA, lacks P10.1) and a single small protein subunit. Bacterial RNase P RNAs are comprised of two independently evolving domains, separated by P7. The RNA upstream and downstream of P7 contains all of the essential catalytic sequences and structures (C-domain). Changes in the RNA bound at each end by the two strands of P7 (the loop of P7) alter substrate specificity (S-domain). The RNA subunit is associated with a single, small conservative protein, encoded by the rnpA gene, which has an unusual left-handed betaalphabeta crossover connection and a large central cleft
physiological function
-
the RNase P holoenzyme is composed of a single RNA (type B3 RNase P RNA, lacks P12) and a single small protein subunit. Bacterial RNase P RNAs are comprised of two independently evolving domains, separated by P7. The RNA upstream and downstream of P7 contains all of the essential catalytic sequences and structures (C-domain). Changes in the RNA bound at each end by the two strands of P7 (the loop of P7) alter substrate specificity (S-domain). The RNA subunit is associated with a single, small conservative protein, encoded by the rnpA gene, which has an unusual left-handed betaalphabeta crossover connection and a large central cleft
physiological function
-
the RNase P holoenzyme is composed of a single RNA (type C RNase P RNA) and a single small protein subunit. Bacterial RNase P RNAs are comprised of two independently evolving domains, separated by P7. The RNA upstream and downstream of P7 contains all of the essential catalytic sequences and structures (C-domain). Changes in the RNA bound at each end by the two strands of P7 (the loop of P7) alter substrate specificity (S-domain). The RNA subunit is associated with a single, small conservative protein, encoded by the rnpA gene, which has an unusual left-handed betaalphabeta crossover connection and a large central cleft
physiological function
-
the RNase P holoenzyme is composed of a single RNA molecule (type A RNase P RNA) and several protein subunits
physiological function
-
the RNase P holoenzyme is composed of a single RNA molecule (type M RNase P RNA, lacking P6, P8, P16 and P17) and several protein subunits
physiological function
-
the RNase P holoenzyme is composed of a single RNA molecule (type T RNase P RNA, lacking the S-domain) and several protein subunits
physiological function
-
Bacillus subtilis RNase P, composed of a catalytically active RNA, PRNA, and a small protein, the P protein, subunit, catalyzes the 5' end maturation of precursor tRNAs. Inner-sphere coordination of divalent metal ions to PRNA is essential for catalytic activity, but not for the formation of the RNase P/pre-tRNA complex. Previous studies have demonstrated that this RNase P/pre-tRNA complex undergoes an essential conformational change before the cleavage step. The RNase P/pre-tRNA conformer is stabilized by a high affinity divalent cation capable of inner-sphere coordination, such as Ca2+ or Mg2+. A second, lower affinity Mg2+ activates cleavage catalyzed by RNase P. Conformational changes and structural analysis, overview
physiological function
-
nuclear RNase P is required for transcription and processing of tRNA
physiological function
RNase P catalyzes 5'-maturation of tRNAs. Recombinant Ostreococcus tauri RPP can functionally reconstitute with bacterial RNase P RNAs but not with Ostreococcus tauri organellar RPRs, despite the latter's presumed bacterial origin
physiological function
-
RNase P is a catalytic ribonucleoprotein primarily involved in tRNA biogenesis. Insights into the role of protein cofactors RPPs in substrate recognition and cleavage-site selection. Cleavage of various model hairpin loop substrates in the presence of archaeal RPPs
physiological function
-
RNase P is a ubiquitous and essential endoribonuclease. It is a catalytic ribonucleoprotein complex that employs an RNA catalyst and Mg2+ ions to cleave precursor RNAs (pre-RNAs) and generate the 5' termini of mature RNAs such as tRNA, 4.5S RNA, tmRNA, and other cellular RNAs
physiological function
-
RNase P is an essential endoribonuclease processing the 59 leader of pre-tRNAs. Compared to bacterial RNase P, which contains a single small protein subunit and a large catalytic RNA subunit, eukaryotic nuclear RNase P is more complex, containing nine proteins and an RNA subunit in Saccharomyces cerevisiae. Nuclear RNase P has been shown to possess unique RNA binding capabilities, molecular recognition of nuclear RNase P, overview. Multiple interactions are required for high affinity binding
physiological function
-
RNase P is an essential endoribonuclease that catalyzes the cleavage of the 59 leader of pre-tRNAs. In addition, a growing number of non-tRNA substrates are identified in various organisms. RNase P varies in composition, as bacterial RNase P contains a catalytic RNA core and one protein subunit, while eukaryotic nuclear RNase P retains the catalytic RNA but has at least nine protein subunits. The additional eukaryotic protein subunits most likely provide additional functionality to RNase P, with one possibility being additional RNA recognition capabilities
physiological function
-
RNase P plays a role in precursor tRNA processing
physiological function
-
RNase P plays a role in precursor tRNA processing
physiological function
-
RNase P plays a role in precursor tRNA processing
physiological function
-
RNase P plays a role in precursor tRNA processing
physiological function
-
RNase P plays a role in precursor tRNA processing
physiological function
-
RNase P plays a role in precursor tRNA processing
physiological function
-
RNase P plays a role in precursor tRNA processing
physiological function
-
RNase P plays a role in precursor tRNA processing
physiological function
-
RNase P plays a role in precursor tRNA processing
physiological function
-
RNase P processes tRNAs by cleavage of precursor-tRNAs. RNase P is a ribozyme. The RNA component catalyzes tRNA maturation in vitro without proteins
physiological function
-
RNase P processes tRNAs by cleavage of precursor-tRNAs. RNase P is a ribozyme. The RNA component catalyzes tRNA maturation in vitro without proteins
physiological function
-
RNase P processes tRNAs by cleavage of precursor-tRNAs. RNase P is a ribozyme. The RNA component catalyzes tRNA maturation in vitro without proteins
physiological function
-
the RNR motif of RNase P protein interacts with both catalytic RNA PRNA and pre-tRNA to stabilize an active conformer
physiological function
-
the stem loops of the RNase P RNA are required as binding sites for the proteins, their interactions are predominantly involved in stabilizing the active conformation of the enzyme
physiological function
-
the ubiquitous endonuclease RNase P is responsible for the 5' maturation of tRNA precursors. In Arabidopsis thaliana mitochondria and plastids, a single protein called proteinaceous RNase P, PRORP1, can perform the endonucleolytic maturation of tRNA precursors that defines RNase P activity. In addition, PRORP1 is able to cleave tRNA-like structures involved in the maturation of plant mitochondrial mRNAs
physiological function
-
ribonuclease P is a ribonucleoprotein complex involved in the processing of the 5'-leader sequence of precursor tRNA (pre-tRNA). RNaseP proteins are predominantly involved in optimization of the pRNA conformation, though they are individually dispensable for RNase P activity in vitro
physiological function
-
the enzyme is involved in the procvessing of the leader sequence of precursor tRNA
physiological function
-
ribonuclease P catalyzes the metal-dependent 5' end maturation of precursor tRNAs
physiological function
-
RNase P is the endonuclease that removes 5' extensions from tRNA precursors, an early and essential step in tRNA biogenesis. PRORP1 Is able to substitute for Saccharomyces cerevisiae strain BY4743 nuclear RNase P in vivo, the inherently different physical qualities of the two enzyme forms are not reflected in a basically different functionality
physiological function
-
the enzyme catalyzes the 5' end maturation of precursor tRNAs
physiological function
-
the enzyme catalyzes the maturation of the 5' end of precursor-tRNAs
physiological function
-
the enzyme catalyzes the maturation of the 5' end of precursor-tRNAs
physiological function
-
the enzyme catalyzes the maturation of the 5' end of precursor-tRNAs
physiological function
-
the enzyme catalyzes the maturation of the 5' end of precursor-tRNAs
physiological function
-
the enzyme catalyzes the maturation of the 5' end of precursor-tRNAs
physiological function
the enzyme catalyzes the maturation of the 5' end of precursor-tRNAs
physiological function
-
the enzyme catalyzes the maturation of the 5' end of precursor-tRNAs. Trypanosoma brucei proteinaceous enzyme PRORP1 can substitute for yeast nuclear RNase P in vivo. Proteinaceous PRORP1 catalyzes all of the other noncanonical, yet vital functions of nuclear yeast RNase P, which may include processing of non-canonical RNAs
physiological function
-
the enzyme catalyzes the Mg2+-dependent 5'-maturation of precursor tRNAs
physiological function
-
the enzyme catalyzes the Mg2+-dependent 5'-maturation of precursor tRNAs
physiological function
-
the enzyme catalyzes the Mg2+-dependent 5'-maturation of precursor tRNAs
physiological function
-
the enzyme catalyzes tRNA 5' maturation
physiological function
-
the enzyme is a ribonuleoprotein that catalyzes the processing of 5' leader sequences from tRNA precursors and other noncoding RNA in all living cells
physiological function
-
the enzyme is an essential ribonucleoprotein enzyme that is responsible for catalyzing the maturation of the 5' end of transfer RNAs through site-specific hydrolysis of a phosphodiester bond in precursor tRNAs. The single enzyme processes the 5' ends of tRNA precursors in cells and organelles that carry out tRNA biosynthesis. Rates of ptRNA processing by RNase P are tuned for uniform specificity and consequently optimal coupling to precursor biosynthesis
physiological function
the enzyme is an RNA-based enzyme primarily responsible for 5'-end pre-tRNA processing
physiological function
-
the enzyme is essential
physiological function
-
the enzyme is required for the initial separation of all seven valine tRNAs from three distinct polycistronic transcripts, the processing of the seven valine tRNAs in Escherichia coli demands special features of the enzyme. Processing of the valU polycistronic transcript is completely dependent on RNase P. Processing of the lysT polycistronic operon requires RNase P but is stimulated by RNase E, EC 3.1.26.12
physiological function
-
the enzyme RNase P is a tRNA processing enzyme. The enzyme can mediate inhibition of human cytomegalovirus gene expression and replication in U373MG cells, and the viral capsid formation, induced by engineered external guide sequences, overview. External guide sequences (EGSs) are RNA molecules that can bind to a target mRNA and direct ribonuclease P for specific cleavage of the target mRNA. Construction of EGS variants that efficiently direct human RNase P to cleave a target mRNA, coding for human cytomegalovirus capsid scaffolding protein and assemblin, in vitro. The EGS variant is about 40fold more active in directing human enzyme to cleave the mRNA in vitro than the EGS derived from a natural tRNA
physiological function
-
the mutant enzyme variant is more effective in HIV RNA sequence cleavage and reducing HIV-1 p24 expression and intracellular viral RNA level in cells than the wild-type ribozyme. A reduction of about 90% in viral RNA level and a reduction of 150fold in viral growth are observed in human H9 cells that express the mutant, while a reduction of less than 10% is observed in H9 cells that either do not express the ribozyme or produce a catalytically inactive ribozyme mutant
physiological function
-
the principle task of the ubiquitous enzyme RNase P is the generation of mature tRNA 5'-ends by removing precursor sequences from tRNA primary transcripts
physiological function
-
the principle task of the ubiquitous enzyme RNase P is the generation of mature tRNA 5'-ends by removing precursor sequences from tRNA primary transcripts
physiological function
-
the principle task of the ubiquitous enzyme RNase P is the generation of mature tRNA 5'-ends by removing precursor sequences from tRNA primary transcripts
physiological function
-
the principle task of the ubiquitous enzyme RNase P is the generation of mature tRNA 5'-ends by removing precursor sequences from tRNA primary transcripts
physiological function
-
the ribonucleoprotein endoribonuclease is responsible for 5' maturation of precursor tRNA
physiological function
the enzyme is involved in maturation of the 5'-end of tRNA
physiological function
-
maturation of tRNA depends on a single endonuclease, ribonuclease P, to remove highly variable 5' leader sequences from precursor tRNA transcripts
physiological function
the enzyme catalyzes 5'-end processing of tRNA
physiological function
the enzyme is involved in the 5' end processing of pre-tRNAs
physiological function
the enzyme is involved maturation of tRNAs by endonucleolytic cleavage of the pre-tRNA
physiological function
-
the enzyme removes the 5'-leader sequence from tRNA precursors
physiological function
-
RNase P catalyzes 5'-maturation of tRNAs. Recombinant Ostreococcus tauri RPP can functionally reconstitute with bacterial RNase P RNAs but not with Ostreococcus tauri organellar RPRs, despite the latter's presumed bacterial origin
-
physiological function
-
the enzyme is involved maturation of tRNAs by endonucleolytic cleavage of the pre-tRNA
-
physiological function
-
the enzyme is involved in the 5' end processing of pre-tRNAs
-
physiological function
-
the enzyme is required for the initial separation of all seven valine tRNAs from three distinct polycistronic transcripts, the processing of the seven valine tRNAs in Escherichia coli demands special features of the enzyme. Processing of the valU polycistronic transcript is completely dependent on RNase P. Processing of the lysT polycistronic operon requires RNase P but is stimulated by RNase E, EC 3.1.26.12
-
physiological function
-
the stem loops of the RNase P RNA are required as binding sites for the proteins, their interactions are predominantly involved in stabilizing the active conformation of the enzyme
-
physiological function
-
the enzyme is involved in the procvessing of the leader sequence of precursor tRNA
-
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
-
additional information
-
Arabidopsis thaliana PRORP1 can replace the bacterial ribonucleoprotein RNase P in Escherichia coli cells
additional information
-
in bacteria, RNase P is composed of a catalytic RNA, PRNA, and a protein subunit, P protein, necessary for function in vivo. The P protein enhances pre-tRNA affinity, selectivity, and cleavage efficiency, as well as modulates the cation requirement for RNase P function. The RNR motif enhances a metal-stabilized conformational change in RNase P that accompanies substrate binding and is essential for efficient catalysis
additional information
-
RNas P RNA solution structure determination using small angle X-ray scattering and selective 29-hydroxyl acylation analyzed by primer extension, SHAPE, analysis, generation of all-atom RNA models, overview. Ab initio modeling fails to define unique scattering envelopes
additional information
-
RNas P RNA solution structure determination using small angle X-ray scattering and selective 29-hydroxyl acylation analyzed by primer extension, SHAPE, analysis, generation of all-atom RNA models, overview. Ab initio modeling fails to define unique scattering envelopes
additional information
-
RNas P RNA solution structure determination using small angle X-ray scattering and selective 29-hydroxyl acylation analyzed by primer extension, SHAPE, analysis, generation of all-atom RNA models, overview. Ab initio modeling fails to define unique scattering envelopes
additional information
-
the catalytic RNP has an H1 RNA moiety associated with ten distinct protein subunits. Five out of eight of these protein subunits, Rpp20, Rpp21, Rpp25, Rpp29, and Pop5, prepared in refolded recombinant forms, bind to H1 RNA in vitro. Rpp20 and Rpp25 bind jointly to H1 RNA, even though each protein can interact independently with this transcript. Nuclease footprinting analysis reveals that Rpp20 and Rpp25 recognize overlapping regions in the P2 and P3 domains of H1 RNA. Rpp21 and Rpp29, which are sufficient for reconstitution of the endonucleolytic activity, bind to separate regions in the catalytic domain of H1 RNA, subunit binding site analysis on H1 RNA, overview
additional information
-
the Pyrobaculum sp. RNase P RNA is about 50% smaller compared to other archaeal RNase Ps
additional information
-
all existing bacterial versions of the rnpA sequence might retain the elements required for functional interaction with the RNase P RNA. But the similarity of the heterologue to the endogenous version does not predict the fitness costs of the replacement
additional information
Arabidopsis thaliana contains a protein only form of RNase P, modeling of PRORP-tRNA interaction
additional information
-
Arabidopsis thaliana contains a protein only form of RNase P, modeling of PRORP-tRNA interaction
additional information
-
in bacteria, RNase P is composed of a catalytic RNA and a protein subunit (P protein) necessary for function in vivo. The P protein enhances pre-tRNA affinity, selectivity, and cleavage efficiency, as well as modulates the cation requirement for RNase P function. The two residues R60 and R62 in the most highly conserved region of the P protein, the RNR motif formed by residues R60-R68, stabilize PRNA complexes with both P protein and pre-tRNA, overview. The RNR motif enhances a metal-stabilized conformational change in RNase P that accompanies substrate binding and is essential for efficient catalysis
additional information
-
in bacteria, the enzyme is a ribonucleoprotein composed of two essential subunits: a catalytic RNA subunit (P RNA, 350-400 nt) and a single small protein cofactor, P protein, secondary structure and tertiary interactions, overview. The RNA subunit of bacterial RNase P is an efficient catalyst in vitro in the absence of its single protein cofactor, while the protein cofactor is essential for RNase P function in vivo, affecting the structure, function, and kinetics of the holoenzyme under physiological salt conditions. In vitro, the protein subunit is dispensable, but its absence has to be compensated for by increased mono- and particularly divalent cations in order to achieve effi cient RNA-alone catalysis
additional information
-
in bacteria, the enzyme is a ribonucleoprotein composed of two essential subunits: a catalytic RNA subunit and a single small protein cofactor, P protein, secondary structure and tertiary interactions, overview. The RNA subunit of bacterial RNase P is an efficient catalyst in vitro in the absence of its single protein cofactor, while the protein cofactor is essential for RNase P function in vivo, affecting the structure, function, and kinetics of the holoenzyme under physiological salt conditions. In vitro, the protein subunit is dispensable, but its absence has to be compensated for by increased mono- and particularly divalent cations in order to achieve efficient RNA-alone catalysis
additional information
-
in bacteria, the enzyme is a ribonucleoprotein composed of two essential subunits: a catalytic RNA subunit and a single small protein cofactor, P protein, secondary structure and tertiary interactions, overview. The RNA subunit of bacterial RNase P is an efficient catalyst in vitro in the absence of its single protein cofactor, while the protein cofactor is essential for RNase P function in vivo, affecting the structure, function, and kinetics of the holoenzyme under physiological salt conditions. In vitro, the protein subunit is dispensable, but its absence has to be compensated for by increased mono- and particularly divalent cations in order to achieve efficient RNA-alone catalysis
additional information
-
in plants, the protein Pop1p is associated with MRP RNAs, i.e. mitochondrial RNA processing RNAs which cleave the large rRNA precursor at the A3 site, and with the catalytic subunit of enzyme RNase P, either separately or in a single large complex. Pop1p-specific antibodies precipitate RNase P activity from wheat extracts. The eukaryotic RNase P consensus sequence with CR II and CR III that are signature elements specific for RNase P RNA
additional information
L0N807
in plants, the protein Pop1p is associated with MRP RNAs, i.e. mitochondrial RNA processing RNAs which cleave the large rRNA precursor at the A3 site, and with the catalytic subunit of enzyme RNase P, either separately or in a single large complex. The eukaryotic RNase P consensus sequence with CR II and CR III that are signature elements specific for RNase P RNA
additional information
-
modeling of RNP-based RNase P
additional information
-
modeling of RNP-based RNase P
additional information
-
modeling of RNP-based RNase P
additional information
-
modeling of RNP-based RNase P
additional information
-
modeling of RNP-based RNase P
additional information
-
RNase P-mediated inhibition of gene expression represents a novel and promising nucleic acid-based gene interference strategy for specific inhibition of target mRNA, overview
additional information
structure-function analysis of proteinaceous RNase P, i.e. the enzyme consisting of only a protein part without catalytic RNA. The anticodon domain of transfer RNA is dispensable, whereas individual residues in D and TpsiC loops are essential for enzyme function, enzyme/transfer RNA interaction, mode of action of the proteinaceous enzyme, overview. Transfer RNA recognition by the proteinaceous PRORP enzyme is similar to that by ribonucleoprotein RNase P enzyme
additional information
-
the enzyme is a ribonlucleoprotein, the RNAsubunit, termed P RNA, contains the active site, whereas the smaller protein subunit is required for optimal molecular recognition and catalysis in vitro and is essential in vivo
additional information
-
the enzyme is a ribonucleoprotein consisting of one protein and one RNA subunit, referred to as C5 and RNase P RNA, respectively. The RNase P RNA is composed of domains that have different functions, the structural architecture of the -1/+73 plays a significant role where a C-1/G+73 pair has the most dramatic effect on kobs
additional information
-
the enzyme is composed of RNA and five proteins (UniProtIDs: O59425, O59150, O59543, and O59248), the proteins assists the RNA part in attaining a functionally active conformation via a distinct mode of binding. Three archaeal proteins, PhoPop5, PhoRpp29, and PhoRpp30, are capable of promoting both, RNA annealing and displacement activities. They function as RNA chaperones or RNA annealers, fluorescence spectrometric analysis, overview. Protein PhoRpp21 shows low activity as annealer, and proein PhoRpp38 is inactive in annealing and strand displacement
additional information
-
the enzyme is composed of two proteins, which localize to the nucleus and the mitochondrion, respectively, and have RNase P activity each on their own. The proteins PRORP1 and PRORP2 are the sole forms of RNase P in trypanosomatids
additional information
-
the metal-dependent conformational change re-organizes the bound substrate in the active site to form a catalytically competent RNase P-pre-tRNA complex
additional information
-
the organellar RNase P RNAs are expressed in vivo, however under in vitro conditions, catalysis of pre-tRNA cleavage is not observed even when associated with the nuclear encoded bacterial-like protein. Modeling of PRORP-tRNA interaction and RNP-based RNase P
additional information
-
the two protein subunits StPop5 and StRpp25 are associated with with floral bud enzyme activity but not with leaf enzyme activity
additional information
wild-type and mutant enzyme structure-function analysis, overview. RNA U52 and two bacterially conserved protein residues, F17 and R89, are essential for efficient Thermotoga maritima enzyme activity. The U52 nucleotide binds a metal ion at the active site, whereas F17 and R89 are positioned over 20 A from the cleavage site, probably making contacts with N-4 and N-5 nucleotides of the pretRNA 5'-leader
additional information
-
wild-type and mutant enzyme structure-function analysis, overview. RNA U52 and two bacterially conserved protein residues, F17 and R89, are essential for efficient Thermotoga maritima enzyme activity. The U52 nucleotide binds a metal ion at the active site, whereas F17 and R89 are positioned over 20 A from the cleavage site, probably making contacts with N-4 and N-5 nucleotides of the pretRNA 5'-leader
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
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100500
-
1 * 120000, RNA subunit, + 1 * 100500, protein subunit Pop1p, + 1 * 22600, protein subunit Pop3p, 1 * 32900, protein subunit Pop4p, + 1 * 19600, protein subunit Pop5p, + 1 * 18200, protein subunit Pop6p, + 1 * 15800, protein subunit Pop7p, + 1 * 15500, protein subunit Pop8p, + 1 * 32200, protein subunit Rpp1p, + 1 * 16300, protein subunit Rpr2p, or 1 * 112000, RNA subunit NME1, + 1 * 22500, protein subunit SNM1
112000
-
1 * 120000, RNA subunit, + 1 * 100500, protein subunit Pop1p, + 1 * 22600, protein subunit Pop3p, 1 * 32900, protein subunit Pop4p, + 1 * 19600, protein subunit Pop5p, + 1 * 18200, protein subunit Pop6p, + 1 * 15800, protein subunit Pop7p, + 1 * 15500, protein subunit Pop8p, + 1 * 32200, protein subunit Rpp1p, + 1 * 16300, protein subunit Rpr2p, or 1 * 112000, RNA subunit NME1, + 1 * 22500, protein subunit SNM1
115000
-
1 * 115000, protein subunit Pop1, + 1 * 40000, protein subunit Rpp40, + 1 * 38000, protein subunit Rpp38, + 1 * 30000, protein subunit Rpp30 or Rpp1, + 1 * 29000, protein subunit Rpp29 or Pop4, + 1 * 25000, protein subunit Rpp25, + 1 * 21000, protein subunit Rpp21 or Rpr2, + 1 * 20000, protein subunit Rpp20 or Pop7 or Rpp2, + 1 * 14000, protein subunit Rpp14, + 1 * 105000, RNA subunit H1
120000
-
1 * 120000, RNA subunit, + 1 * 100500, protein subunit Pop1p, + 1 * 22600, protein subunit Pop3p, 1 * 32900, protein subunit Pop4p, + 1 * 19600, protein subunit Pop5p, + 1 * 18200, protein subunit Pop6p, + 1 * 15800, protein subunit Pop7p, + 1 * 15500, protein subunit Pop8p, + 1 * 32200, protein subunit Rpp1p, + 1 * 16300, protein subunit Rpr2p, or 1 * 112000, RNA subunit NME1, + 1 * 22500, protein subunit SNM1
125000
-
1 * 19000, + 1 * 21000, + 1 * 30000, + 1 * 33000, + 1 * 45000, + 1 * 85000, + 1 * 125000, polypeptides, + 1 * ?, RNA component, SDS-PAGE
13000
-
P protein plus 400 nt RNA subunit
13200
-
2 * 16000, full-length Rpp20, gel filtration. 2 * 14100, Rpp20(16-140), gel filtration. 2 * 13200, HisRpp20(35-140), gel filtration
13800
-
1 * 13800 + 1 * ?, the enzyme is composed of an RNA called M1 which is 377 nucleotides long and a very basic protein of 13800 Da, called C5. Both subunits are present in the molar ratio 1:1
14000
-
1 * 115000, protein subunit Pop1, + 1 * 40000, protein subunit Rpp40, + 1 * 38000, protein subunit Rpp38, + 1 * 30000, protein subunit Rpp30 or Rpp1, + 1 * 29000, protein subunit Rpp29 or Pop4, + 1 * 25000, protein subunit Rpp25, + 1 * 21000, protein subunit Rpp21 or Rpr2, + 1 * 20000, protein subunit Rpp20 or Pop7 or Rpp2, + 1 * 14000, protein subunit Rpp14, + 1 * 105000, RNA subunit H1
14100
-
2 * 16000, full-length Rpp20, gel filtration. 2 * 14100, Rpp20(16-140), gel filtration. 2 * 13200, HisRpp20(35-140), gel filtration
15400
-
mutant Rpp25(25-170), gel filtration
15500
-
1 * 120000, RNA subunit, + 1 * 100500, protein subunit Pop1p, + 1 * 22600, protein subunit Pop3p, 1 * 32900, protein subunit Pop4p, + 1 * 19600, protein subunit Pop5p, + 1 * 18200, protein subunit Pop6p, + 1 * 15800, protein subunit Pop7p, + 1 * 15500, protein subunit Pop8p, + 1 * 32200, protein subunit Rpp1p, + 1 * 16300, protein subunit Rpr2p, or 1 * 112000, RNA subunit NME1, + 1 * 22500, protein subunit SNM1
15800
-
1 * 120000, RNA subunit, + 1 * 100500, protein subunit Pop1p, + 1 * 22600, protein subunit Pop3p, 1 * 32900, protein subunit Pop4p, + 1 * 19600, protein subunit Pop5p, + 1 * 18200, protein subunit Pop6p, + 1 * 15800, protein subunit Pop7p, + 1 * 15500, protein subunit Pop8p, + 1 * 32200, protein subunit Rpp1p, + 1 * 16300, protein subunit Rpr2p, or 1 * 112000, RNA subunit NME1, + 1 * 22500, protein subunit SNM1
16300
-
1 * 120000, RNA subunit, + 1 * 100500, protein subunit Pop1p, + 1 * 22600, protein subunit Pop3p, 1 * 32900, protein subunit Pop4p, + 1 * 19600, protein subunit Pop5p, + 1 * 18200, protein subunit Pop6p, + 1 * 15800, protein subunit Pop7p, + 1 * 15500, protein subunit Pop8p, + 1 * 32200, protein subunit Rpp1p, + 1 * 16300, protein subunit Rpr2p, or 1 * 112000, RNA subunit NME1, + 1 * 22500, protein subunit SNM1
170000
-
rate-zonal sedimentation in linear isokinetic glycerol gradients
17500
-
x * 17500, SDS-PAGE
18200
-
1 * 120000, RNA subunit, + 1 * 100500, protein subunit Pop1p, + 1 * 22600, protein subunit Pop3p, 1 * 32900, protein subunit Pop4p, + 1 * 19600, protein subunit Pop5p, + 1 * 18200, protein subunit Pop6p, + 1 * 15800, protein subunit Pop7p, + 1 * 15500, protein subunit Pop8p, + 1 * 32200, protein subunit Rpp1p, + 1 * 16300, protein subunit Rpr2p, or 1 * 112000, RNA subunit NME1, + 1 * 22500, protein subunit SNM1
19000
-
1 * 19000, + 1 * 21000, + 1 * 30000, + 1 * 33000, + 1 * 45000, + 1 * 85000, + 1 * 125000, polypeptides, + 1 * ?, RNA component, SDS-PAGE
19600
-
1 * 120000, RNA subunit, + 1 * 100500, protein subunit Pop1p, + 1 * 22600, protein subunit Pop3p, 1 * 32900, protein subunit Pop4p, + 1 * 19600, protein subunit Pop5p, + 1 * 18200, protein subunit Pop6p, + 1 * 15800, protein subunit Pop7p, + 1 * 15500, protein subunit Pop8p, + 1 * 32200, protein subunit Rpp1p, + 1 * 16300, protein subunit Rpr2p, or 1 * 112000, RNA subunit NME1, + 1 * 22500, protein subunit SNM1
20000
-
1 * 115000, protein subunit Pop1, + 1 * 40000, protein subunit Rpp40, + 1 * 38000, protein subunit Rpp38, + 1 * 30000, protein subunit Rpp30 or Rpp1, + 1 * 29000, protein subunit Rpp29 or Pop4, + 1 * 25000, protein subunit Rpp25, + 1 * 21000, protein subunit Rpp21 or Rpr2, + 1 * 20000, protein subunit Rpp20 or Pop7 or Rpp2, + 1 * 14000, protein subunit Rpp14, + 1 * 105000, RNA subunit H1
20600
-
mutant Rpp25, gel filtration
20700
-
mutant Rpp25(25-170), sequence analysis
21500
L0N807
x * 21500, AtPop1 protein, two spliced exons encoding a 190 residues long protein, starting from AUG1 from gene At2G47290, SDS-PAGE
22500
-
1 * 120000, RNA subunit, + 1 * 100500, protein subunit Pop1p, + 1 * 22600, protein subunit Pop3p, 1 * 32900, protein subunit Pop4p, + 1 * 19600, protein subunit Pop5p, + 1 * 18200, protein subunit Pop6p, + 1 * 15800, protein subunit Pop7p, + 1 * 15500, protein subunit Pop8p, + 1 * 32200, protein subunit Rpp1p, + 1 * 16300, protein subunit Rpr2p, or 1 * 112000, RNA subunit NME1, + 1 * 22500, protein subunit SNM1
22600
-
1 * 120000, RNA subunit, + 1 * 100500, protein subunit Pop1p, + 1 * 22600, protein subunit Pop3p, 1 * 32900, protein subunit Pop4p, + 1 * 19600, protein subunit Pop5p, + 1 * 18200, protein subunit Pop6p, + 1 * 15800, protein subunit Pop7p, + 1 * 15500, protein subunit Pop8p, + 1 * 32200, protein subunit Rpp1p, + 1 * 16300, protein subunit Rpr2p, or 1 * 112000, RNA subunit NME1, + 1 * 22500, protein subunit SNM1
232000
-
glycerol density gradient sedimentation
24000
-
1 * 55000 + 1 * 41000, + 1 * 40000, + 1 * 26000, 1 * 24000, + 1 * 18000, + 1 * 16000, polypeptides, + 1 * 76000, RNA subunit, the enzyme is composed of seven polypeptides and an RNA moiety, the RNA component affects significantly the hydrodynamic properties of the RNase P enzyme, resulting in overestimation of the size of the ribonucleoprotein in gel filtration, SDS-PAGE
25000
-
1 * 115000, protein subunit Pop1, + 1 * 40000, protein subunit Rpp40, + 1 * 38000, protein subunit Rpp38, + 1 * 30000, protein subunit Rpp30 or Rpp1, + 1 * 29000, protein subunit Rpp29 or Pop4, + 1 * 25000, protein subunit Rpp25, + 1 * 21000, protein subunit Rpp21 or Rpr2, + 1 * 20000, protein subunit Rpp20 or Pop7 or Rpp2, + 1 * 14000, protein subunit Rpp14, + 1 * 105000, RNA subunit H1
26400
-
mutant HisRpp20(35-140), gel filtration
28100
-
mutant Rpp20(16-140), gel filtration
28600
-
mutant Rpp20(35-140)/Rpp25(25-170), gel filtration
29000
-
1 * 115000, protein subunit Pop1, + 1 * 40000, protein subunit Rpp40, + 1 * 38000, protein subunit Rpp38, + 1 * 30000, protein subunit Rpp30 or Rpp1, + 1 * 29000, protein subunit Rpp29 or Pop4, + 1 * 25000, protein subunit Rpp25, + 1 * 21000, protein subunit Rpp21 or Rpr2, + 1 * 20000, protein subunit Rpp20 or Pop7 or Rpp2, + 1 * 14000, protein subunit Rpp14, + 1 * 105000, RNA subunit H1
31100
-
mutant Rpp20(35-140)/Rpp25(25-170), sequence analysis
31500
-
mutant Rpp20/Rpp25(25-170), gel filtration
32100
-
full-length Rpp20, gel filtration
32200
-
1 * 120000, RNA subunit, + 1 * 100500, protein subunit Pop1p, + 1 * 22600, protein subunit Pop3p, 1 * 32900, protein subunit Pop4p, + 1 * 19600, protein subunit Pop5p, + 1 * 18200, protein subunit Pop6p, + 1 * 15800, protein subunit Pop7p, + 1 * 15500, protein subunit Pop8p, + 1 * 32200, protein subunit Rpp1p, + 1 * 16300, protein subunit Rpr2p, or 1 * 112000, RNA subunit NME1, + 1 * 22500, protein subunit SNM1
32900
-
1 * 120000, RNA subunit, + 1 * 100500, protein subunit Pop1p, + 1 * 22600, protein subunit Pop3p, 1 * 32900, protein subunit Pop4p, + 1 * 19600, protein subunit Pop5p, + 1 * 18200, protein subunit Pop6p, + 1 * 15800, protein subunit Pop7p, + 1 * 15500, protein subunit Pop8p, + 1 * 32200, protein subunit Rpp1p, + 1 * 16300, protein subunit Rpr2p, or 1 * 112000, RNA subunit NME1, + 1 * 22500, protein subunit SNM1
36600
-
mutant Rpp20/Rpp25, gel filtration
38000
-
1 * 115000, protein subunit Pop1, + 1 * 40000, protein subunit Rpp40, + 1 * 38000, protein subunit Rpp38, + 1 * 30000, protein subunit Rpp30 or Rpp1, + 1 * 29000, protein subunit Rpp29 or Pop4, + 1 * 25000, protein subunit Rpp25, + 1 * 21000, protein subunit Rpp21 or Rpr2, + 1 * 20000, protein subunit Rpp20 or Pop7 or Rpp2, + 1 * 14000, protein subunit Rpp14, + 1 * 105000, RNA subunit H1
39200
-
mutant Rpp25, sequence analysis
39900
-
mutant HisRpp20(35-140), sequence analysis
41000
-
1 * 55000 + 1 * 41000, + 1 * 40000, + 1 * 26000, 1 * 24000, + 1 * 18000, + 1 * 16000, polypeptides, + 1 * 76000, RNA subunit, the enzyme is composed of seven polypeptides and an RNA moiety, the RNA component affects significantly the hydrodynamic properties of the RNase P enzyme, resulting in overestimation of the size of the ribonucleoprotein in gel filtration, SDS-PAGE
41100
-
mutant Rpp20/Rpp25(25-170), sequence analysis
44400
-
mutant [Rpp20(35-140)-Rpp25(25-170)]/P3 RNA, gel filtration
45300
-
mutant Rpp20(16-140), sequence analysis
47000
-
full-length Rpp20, sequence analysis
52500
-
mutant [Rpp20-Rpp25]/P3 RNA, gel filtration
53800
-
mutant Rpp20/Rpp25, sequence analysis
55000
-
1 * 55000 + 1 * 41000, + 1 * 40000, + 1 * 26000, 1 * 24000, + 1 * 18000, + 1 * 16000, polypeptides, + 1 * 76000, RNA subunit, the enzyme is composed of seven polypeptides and an RNA moiety, the RNA component affects significantly the hydrodynamic properties of the RNase P enzyme, resulting in overestimation of the size of the ribonucleoprotein in gel filtration, SDS-PAGE
56400
-
mutant [Rpp20(35-140)-Rpp25(25-170)]/P3 RNA, sequence analysis
580000
-
glycerol density gradient sedimentation analysis, gel filtration
71400
-
mutant [Rpp20-Rpp25]/P3 RNA, sequence analysis
76000
-
1 * 55000 + 1 * 41000, + 1 * 40000, + 1 * 26000, 1 * 24000, + 1 * 18000, + 1 * 16000, polypeptides, + 1 * 76000, RNA subunit, the enzyme is composed of seven polypeptides and an RNA moiety, the RNA component affects significantly the hydrodynamic properties of the RNase P enzyme, resulting in overestimation of the size of the ribonucleoprotein in gel filtration, SDS-PAGE
85000
-
1 * 19000, + 1 * 21000, + 1 * 30000, + 1 * 33000, + 1 * 45000, + 1 * 85000, + 1 * 125000, polypeptides, + 1 * ?, RNA component, SDS-PAGE
105000
-
mitochondrial enzyme
105000
-
1 * 115000, protein subunit Pop1, + 1 * 40000, protein subunit Rpp40, + 1 * 38000, protein subunit Rpp38, + 1 * 30000, protein subunit Rpp30 or Rpp1, + 1 * 29000, protein subunit Rpp29 or Pop4, + 1 * 25000, protein subunit Rpp25, + 1 * 21000, protein subunit Rpp21 or Rpr2, + 1 * 20000, protein subunit Rpp20 or Pop7 or Rpp2, + 1 * 14000, protein subunit Rpp14, + 1 * 105000, RNA subunit H1
16000
-
1 * 55000 + 1 * 41000, + 1 * 40000, + 1 * 26000, 1 * 24000, + 1 * 18000, + 1 * 16000, polypeptides, + 1 * 76000, RNA subunit, the enzyme is composed of seven polypeptides and an RNA moiety, the RNA component affects significantly the hydrodynamic properties of the RNase P enzyme, resulting in overestimation of the size of the ribonucleoprotein in gel filtration, SDS-PAGE
16000
-
2 * 16000, full-length Rpp20, gel filtration. 2 * 14100, Rpp20(16-140), gel filtration. 2 * 13200, HisRpp20(35-140), gel filtration
18000
-
1 * 55000 + 1 * 41000, + 1 * 40000, + 1 * 26000, 1 * 24000, + 1 * 18000, + 1 * 16000, polypeptides, + 1 * 76000, RNA subunit, the enzyme is composed of seven polypeptides and an RNA moiety, the RNA component affects significantly the hydrodynamic properties of the RNase P enzyme, resulting in overestimation of the size of the ribonucleoprotein in gel filtration, SDS-PAGE
18000
-
x * 18000, recombinant His6-tagged protein StPop5, SDS-PAGE, x * 33000, recombinant His6-tagged protein StRpp25, SDS-PAGE
21000
-
1 * 19000, + 1 * 21000, + 1 * 30000, + 1 * 33000, + 1 * 45000, + 1 * 85000, + 1 * 125000, polypeptides, + 1 * ?, RNA component, SDS-PAGE
21000
-
1 * 115000, protein subunit Pop1, + 1 * 40000, protein subunit Rpp40, + 1 * 38000, protein subunit Rpp38, + 1 * 30000, protein subunit Rpp30 or Rpp1, + 1 * 29000, protein subunit Rpp29 or Pop4, + 1 * 25000, protein subunit Rpp25, + 1 * 21000, protein subunit Rpp21 or Rpr2, + 1 * 20000, protein subunit Rpp20 or Pop7 or Rpp2, + 1 * 14000, protein subunit Rpp14, + 1 * 105000, RNA subunit H1
26000
-
MRPP2
26000
-
1 * 55000 + 1 * 41000, + 1 * 40000, + 1 * 26000, 1 * 24000, + 1 * 18000, + 1 * 16000, polypeptides, + 1 * 76000, RNA subunit, the enzyme is composed of seven polypeptides and an RNA moiety, the RNA component affects significantly the hydrodynamic properties of the RNase P enzyme, resulting in overestimation of the size of the ribonucleoprotein in gel filtration, SDS-PAGE
30000
-
1 * 19000, + 1 * 21000, + 1 * 30000, + 1 * 33000, + 1 * 45000, + 1 * 85000, + 1 * 125000, polypeptides, + 1 * ?, RNA component, SDS-PAGE
30000
-
1 * 115000, protein subunit Pop1, + 1 * 40000, protein subunit Rpp40, + 1 * 38000, protein subunit Rpp38, + 1 * 30000, protein subunit Rpp30 or Rpp1, + 1 * 29000, protein subunit Rpp29 or Pop4, + 1 * 25000, protein subunit Rpp25, + 1 * 21000, protein subunit Rpp21 or Rpr2, + 1 * 20000, protein subunit Rpp20 or Pop7 or Rpp2, + 1 * 14000, protein subunit Rpp14, + 1 * 105000, RNA subunit H1
33000
-
1 * 19000, + 1 * 21000, + 1 * 30000, + 1 * 33000, + 1 * 45000, + 1 * 85000, + 1 * 125000, polypeptides, + 1 * ?, RNA component, SDS-PAGE
33000
-
x * 18000, recombinant His6-tagged protein StPop5, SDS-PAGE, x * 33000, recombinant His6-tagged protein StRpp25, SDS-PAGE
40000
-
1 * 55000 + 1 * 41000, + 1 * 40000, + 1 * 26000, 1 * 24000, + 1 * 18000, + 1 * 16000, polypeptides, + 1 * 76000, RNA subunit, the enzyme is composed of seven polypeptides and an RNA moiety, the RNA component affects significantly the hydrodynamic properties of the RNase P enzyme, resulting in overestimation of the size of the ribonucleoprotein in gel filtration, SDS-PAGE
40000
-
1 * 115000, protein subunit Pop1, + 1 * 40000, protein subunit Rpp40, + 1 * 38000, protein subunit Rpp38, + 1 * 30000, protein subunit Rpp30 or Rpp1, + 1 * 29000, protein subunit Rpp29 or Pop4, + 1 * 25000, protein subunit Rpp25, + 1 * 21000, protein subunit Rpp21 or Rpr2, + 1 * 20000, protein subunit Rpp20 or Pop7 or Rpp2, + 1 * 14000, protein subunit Rpp14, + 1 * 105000, RNA subunit H1
400000
-
gel filtration
400000
-
greater than, gel filtration
400000
-
gel exclusion chromatography
45000
-
about, gel filtration
45000
-
1 * 19000, + 1 * 21000, + 1 * 30000, + 1 * 33000, + 1 * 45000, + 1 * 85000, + 1 * 125000, polypeptides, + 1 * ?, RNA component, SDS-PAGE
70000
-
-
70000
-
gel filtration, mitochondrial enzyme form
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decamer
-
1 * 120000, RNA subunit, + 1 * 100500, protein subunit Pop1p, + 1 * 22600, protein subunit Pop3p, 1 * 32900, protein subunit Pop4p, + 1 * 19600, protein subunit Pop5p, + 1 * 18200, protein subunit Pop6p, + 1 * 15800, protein subunit Pop7p, + 1 * 15500, protein subunit Pop8p, + 1 * 32200, protein subunit Rpp1p, + 1 * 16300, protein subunit Rpr2p, or 1 * 112000, RNA subunit NME1, + 1 * 22500, protein subunit SNM1
heterodimer
-
Rpp20 and Rpp25, ITC-200 microcalorimeter experiments
homodimer
-
2 * 16000, full-length Rpp20, gel filtration. 2 * 14100, Rpp20(16-140), gel filtration. 2 * 13200, HisRpp20(35-140), gel filtration
homooligomer
x * 23000, SDS-PAGE
monomer
-
Rpp25 in solution
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
?
L0N807
x * 21500, AtPop1 protein, two spliced exons encoding a 190 residues long protein, starting from AUG1 from gene At2G47290, SDS-PAGE
?
Chlamydomonas reinhardtii cw15 arg7-8 mt+
-
x * 100000, SDS-PAGE
-
?
-
x * 18000, recombinant His6-tagged protein StPop5, SDS-PAGE, x * 33000, recombinant His6-tagged protein StRpp25, SDS-PAGE
dimer
-
x * 13990-14000, protein subunit, + x * ?, RNA subunit, SDS-PAGE and mass spectrometry
dimer
-
1 * 13800 + 1 * ?, the enzyme is composed of an RNA called M1 which is 377 nucleotides long and a very basic protein of 13800 Da, called C5. Both subunits are present in the molar ratio 1:1
dimer
all bacterial RNase Ps have one RNA and one protein component. A conserved RNR motif in bacterial RNase P protein components is involved in their interaction with the RNA component
dimer
-
all bacterial RNase Ps have one RNA and one protein component. A conserved RNR motif in bacterial RNase P protein components is involved in their interaction with the RNA component
-
octamer
-
1 * 19000, + 1 * 21000, + 1 * 30000, + 1 * 33000, + 1 * 45000, + 1 * 85000, + 1 * 125000, polypeptides, + 1 * ?, RNA component, SDS-PAGE
octamer
-
1 * 55000 + 1 * 41000, + 1 * 40000, + 1 * 26000, 1 * 24000, + 1 * 18000, + 1 * 16000, polypeptides, + 1 * 76000, RNA subunit, the enzyme is composed of seven polypeptides and an RNA moiety, the RNA component affects significantly the hydrodynamic properties of the RNase P enzyme, resulting in overestimation of the size of the ribonucleoprotein in gel filtration, SDS-PAGE
oligomer
-
1 * 115000, protein subunit Pop1, + 1 * 40000, protein subunit Rpp40, + 1 * 38000, protein subunit Rpp38, + 1 * 30000, protein subunit Rpp30 or Rpp1, + 1 * 29000, protein subunit Rpp29 or Pop4, + 1 * 25000, protein subunit Rpp25, + 1 * 21000, protein subunit Rpp21 or Rpr2, + 1 * 20000, protein subunit Rpp20 or Pop7 or Rpp2, + 1 * 14000, protein subunit Rpp14, + 1 * 105000, RNA subunit H1
oligomer
-
enzyme is composed of 1 RNA subunit H1 and at least 9 protein subunits, namely Rpp14, Rpp20, Rpp21, Rpp29 i.e. Pop4, Rpp30, Rpp40, Pop1, Pop5, and Rpp25
oligomer
-
subunit composition and interaction, 1 essential RNA subunit, i.e. H1 for RNase P or 7-2 for RNase MRP, plus 9 protein components namely Pop1p, Rpp29p, Rpp20p, Rpp30p, Rep38p, Rpp40p, Rpp25p, and Rpp14p for RNase P, or pls 4 protein components namely Pop1p, Rpp29p, Rpp20p, and Rpp30p for RNase MRP, overview
oligomer
-
subunit composition, 1 RNA subunit, i.e. H1 for RNase P or 7-2 for RNase MRP, plus 9 protein components namely Pop1p, Rpp29p, Rpp20p, Rpp30p, Rep38p, Rpp40p, Rpp25p, and Rpp14p for RNase P, or pls 4 protein components namely Pop1p, Rpp29p, Rpp20p, and Rpp30p for RNase MRP, overview
oligomer
-
the archaeal holoenzyme is associated with 1 RNase P RNA and at least 4 RNase P proteins (POP5, RPP30, RPP21 and RPP29). Archaeal RNase P proteins function as two binary RNase P protein complexes (POP5/RPP30 and RPP21/RPP29). Archaeal POP5/RPP30 reconstituted with bacterial and organellar RNase P RNAs. While POP5/RPP30 is solely responsible for enhancing the cleavage rate of precursor tRNA by RNase P RNAs (by 60fold), RPP21/RPP29 contributes to increased substrate affinity (by 16fold)
oligomer
-
the archaeal holoenzyme is associated with 1 RNase P RNA and at least 4 RNase P proteins (POP5, RPP30, RPP21 and RPP29). Archaeal RNase P proteins function as two binary RNase P protein complexes (POP5/RPP30 and RPP21/RPP29). Archaeal POP5/RPP30 reconstituted with bacterial and organellar RNase P RNAs. While POP5/RPP30 is solely responsible for enhancing the cleavage rate of precursor tRNA by RNase P RNAs (by 60fold), RPP21/RPP29 contributes to increased substrate affinity (by 16fold)
oligomer
-
a multi-subunit catalytic ribonucleoprotein complex. Step-wise, Mg2+-dependent reconstitutions of Pfu RNaseP with its catalytic RNA subunit and two interacting protein cofactor pairs (RPP21/RPP29 and POP5/RPP30) reveals functional RNP intermediates en route to the RNaseP enzyme 1:1 composition for all subunits when either one or both protein complexes bind the cognate RNA
oligomer
-
the archaeal holoenzyme is associated with 1 RNase P RNA and at least 4 RNase P proteins (POP5, RPP30, RPP21 and RPP29). Archaeal RNase P proteins function as two binary RNase P protein complexes (POP5/RPP30 and RPP21/RPP29). Archaeal POP5/RPP30 reconstituted with bacterial and organellar RNase P RNAs. While POP5/RPP30 is solely responsible for enhancing the cleavage rate of precursor tRNA by RNase P RNAs (by 60fold), RPP21/RPP29 contributes to increased substrate affinity (by 16-fold)
oligomer
-
the RNA-binding protein L7Ae (UniProt: Q8U160) is a subunit of the archaeal RNase P ribonucleoprotein complex. The L7Ae protein binds to two kink-turns in the Pyrococcus furiosus RNase P RNA
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
oligomer
-
the nuclear RNase P complex has 1 RNA subunit and 9 distinct protein subunits essential for cell viability and tRNA processing, RNase MRP contains 8 protein subunit and 1 RNA subunit
additional information
-
RNase P RNA solution structure determination using small angle X-ray scattering and selective 29-hydroxyl acylation analyzed by primer extension, SHAPE, analysis, generation of all-atom RNA models, overview
additional information
-
enzyme secondary structure and tertiary interactions, overview
additional information
-
two aspartates are essential for the activity of PRORP1
additional information
structure homology modelling of the enzyme's PRORP domain with bound pre-tRNACys from Escherichia coli, overview
additional information
-
the mitochondrial enzyme contains an RNA subunit and 7 protein subunits of 16-55 kDa
additional information
-
RNA and protein subunits from one species can complement subunits from the other species in reconstitution experiments
additional information
-
the protein component both alters the conformation of the RNA component and enhances the substrate affinity and specificity
additional information
-
enzyme is composed of 1 RNA subunit of 350-450 nucleotides and 1 protein subunit of about 120 amino acids, the RNA subunit is divided into the specificity and the catalytic domain, i.e. S domain, comprising nucleotides 86-239, and C domain, comprising the rest of the molecule, overall and secondary structure, modeling
additional information
-
enzyme is composed of a large RNA subunit of about 400 nucleotides, and a small protein subunit of about 100 amino acids, global structure of the enzyme-substrate complex
additional information
-
primary and secondary structure of the ribozymal RNA, catalytic domain and specificity domain, structure of the ribozyme plays an important role in catalysis, overview
additional information
-
protein subunit structure, the enzyme folds as an alpha-beta sandwich and has the overall topology of alpha(beta)3alphabetaalpha, tertiary structure, overview
additional information
-
ribozyme structure
additional information
-
subunit composition, 1 large RNA subunit plus 1 small protein subunit contributing to about 10% of the mass of the holoenzyme
additional information
-
protein component influences holoenzyme dimer formation. Protein component does not stabilize the global structure of RNase P RNA. Differences between the two types of holoenzymes of Escherichia coli and Bacillus subtilis reside primarily in the RNA and not the protein components of each
additional information
-
Bacterial RNase P is composed of one RNA (PRNA, ca. 400 nucleotides [nt]) and one small protein subunit (P protein, ca. 120 amino acids)
additional information
-
in bacteria, RNase P is composed of a catalytic RNA, PRNA, and a protein subunit, P protein, necessary for function in vivo. The P protein enhances pre-tRNA affinity, selectivity, and cleavage efficiency, as well as modulates the cation requirement for RNase P function. Two residues, R60 and R62, in the most highly conserved region of the P protein, the RNR motif, R60-R68, stabilize PRNA complexes with both P protein and pre-tRNA. The RNR motif enhances a metal-stabilized conformational change in RNase P that accompanies substrate binding and is essential for efficient catalysis. Stabilization of this conformational change contributes to both the decreased metal requirement and the enhanced substrate recognition of the RNase P holoenzyme, illuminating the role of the most highly conserved region of P protein in the RNase P reaction pathway
additional information
-
enzyme secondary structure and tertiary interactions, overview
additional information
-
ribonuclease P is composed of a catalytically active RNA (PRNA) and a small protein (P protein) subunit
additional information
-
subunit composition, 1 essential RNA subunit
additional information
-
the subunits DRpp29 and RNase P form the holoenzyme RNase P, DRpp29 binds specifically to the RNase P RNA subunit, interaction analysis, overview. An eukaryotic specific, lysine- and arginine-rich region facilitates the interaction between the two subunits. Modeling and prediction of potential RNA binding residues in DRpp29, overview
additional information
-
the subunits DRpp29 and RNase P form the holoenzyme RNase P, DRpp29 binds specifically to the RNase P RNA subunit, interaction analysis, overview. An eukaryotic specific, lysine- and arginine-rich region facilitates the interaction between the two subunits. Modeling and prediction of potential RNA binding residues in DRpp29, overview
-
additional information
-
-
additional information
-
active holoenzymes can be reconstituted from the Thermotoga aquaticus and the Thermotoga maritima RNAs and the protein component of RNase P from Escherichia coli
additional information
-
RNA and protein subunits from one species can complement subunits from the other species in reconstitution experiments
additional information
-
enzyme folding and function are dependent on divalent metal cations, clustered interactions, e.g. with the helix P4 of the enzymes' RNA part, secondary structure of the RNA moiety, overview
additional information
-
enzyme is composed of a large RNA subunit of about 400 nucleotides and a smaller protein subunit
additional information
-
enzyme is composed of a large RNA subunit of about 400 nucleotides, and a small protein subunit of about 100 amino acids, global structure of the enzyme-substrate complex, secondary structure of the enzyme RNA subunit
additional information
-
enzyme secondary structure, domain organization and tertiary structure, modeling, overview
additional information
-
primary and secondary structure of the ribozymal RNA, catalytic domain and specificity domain, structure of the ribozyme plays an important role in catalysis, overview
additional information
-
ribozyme structure
additional information
-
subunit composition, 1 large RNA subunit plus 1 small protein subunit contributing to about 10% of the mass of the holoenzyme
additional information
-
m1 RNA, the catalytic RNA subunit of RNase P is present in two main conformational states, one being characteristic of free RNase P and one of an RNase P-tRNA complex. The C5 protein subunit does not induce the major structural changes
additional information
-
protein stabilizes the global structure of RNase P RNA and influences holoenzyme dimer formation. Differences between the two types of holoenzymes of Escherichia coli and Bacillus subtilis reside primarily in the RNA and not the protein components of each
additional information
-
RNase P RNA solution structure determination using small angle X-ray scattering and selective 29-hydroxyl acylation analyzed by primer extension, SHAPE, analysis, generation of all-atom RNA models, overview
additional information
-
enzyme secondary structure and tertiary interactions, overview
additional information
-
the enzyme is a ribonlucleoprotein, the RNAsubunit, termed P RNA, contains the active site, whereas the smaller protein subunit, i.e. C5 protein, is required for optimal molecular recognition and catalysis in vitro and is essential in vivo
additional information
-
the enzyme is a ribonucleoprotein consisting of one protein and one RNA subunit, referred to as C5 and RNase P RNA, respectively. The RNase P RNA is composed of domains that have different functions
additional information
-
the essential enzyme consists of the C5 protein and the catalytic M1 RNA subunits
additional information
-
the essential enzyme consists of the C5 protein and the catalytic M1 RNA subunits
-
additional information
-
RNase P RNA solution structure determination using small angle X-ray scattering and selective 29-hydroxyl acylation analyzed by primer extension, SHAPE, analysis, generation of all-atom RNA models, overview
additional information
-
autoantigenic properties of the protein subunits Rpp38 and Rpp30 of catalytically active complexes of human ribonuclease P
additional information
-
modeling of RNase P holoenzyme assembly, both the mitochondrial and nuclear enzyme complexes are composed of at least 10 protein subunits and 1 RNA subunit H1, overview
additional information
the RNase P complex for 5'-end cleavage comprises the methyltransferase domain-containing protein tRNA methyltransferase 10C, mitochondrial RNase P subunit (TRMT10C/MRPP1), short-chain oxidoreductase hydroxysteroid 17'-dehydrogenase 10 (HSD17B10/MRPP2), and metallonuclease KIAA0391/MRPP3
additional information
-
the RNase P complex for 5'-end cleavage comprises the methyltransferase domain-containing protein tRNA methyltransferase 10C, mitochondrial RNase P subunit (TRMT10C/MRPP1), short-chain oxidoreductase hydroxysteroid 17'-dehydrogenase 10 (HSD17B10/MRPP2), and metallonuclease KIAA0391/MRPP3
additional information
-
subunit composition, secondary structure of the enzyme RNA moiety
additional information
-
subunit composition, at least 4 protein subunits namely MTH11, MTH687, MTH688, and MTH1618
additional information
-
subunit composition, secondary structure of the enzyme RNA moiety
additional information
-
RNase P contains an essential RNase P RNA and RNase P protein
additional information
-
archaeal RNase P comprises a catalytic RNase P RNA, RPR, and at least four protein cofactors, RPPs, which function as two binary complexes, POP5/RPP30 and RPP21/RPP29
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
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
-
enzyme is a ribonucleoprotein consisting of multiple protein components and a single RNA species
additional information
-
subunit composition for RNase P: 1 RNA subunit RPM1 plus at least 1 protein subunit Rpm2p for the mitochondrial ribozyme, 9 protein components for the nuclear enzyme form, namely Pop1p, Pop3p-Pop8p, Rpp1p, and Rpr2p, secondary structure of nuclear enzyme RNA, subunit composition for RNase MRP: 1 RNA subunit NME1 plus 9 protein components for the nuclear enzyme form, namely Pop1p, Pop3p-Pop7p, Pop, Rpp1p, and SNM1, overview, Pop7p is also known as Rpp2p
additional information
-
subunit interactions, subunit composition for RNase P: 1 RNA subunit RPM1 plus at least 1 protein subunit Rpm2p for the mitochondrial ribozyme, 9 protein components for the nuclear enzyme form, namely Pop1p, Pop3p-Pop8p, Rpp1p, and Rpr2p, secondary structure of nuclear enzyme RNA, subunit composition for RNase MRP: 1 RNA subunit NME1 plus 9 protein components for the nuclear enzyme form, namely Pop1p, Pop3p-Pop7p, Pop, Rpp1p, and SNM1, overview, Pop7p is also known as Rpp2p, structure-function relationship of the RNA subunit
additional information
-
the mitochondrial enzyme contains a single RNa subunit and a single protein subunit
additional information
-
Nuclear RNase P contains one RNA subunit, RPR1 RNA, and nine protein subunits: Pop1p, Pop3p, Pop4p, Pop5p, Pop6p, Pop7p, Pop8p, Rpp1p, and Rpr2p
additional information
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RNase P has nine essential protein components (Pop1, Pop3, Pop4, Pop5, Pop6, Pop7, Pop8, Rpp1 and Rpr2)
additional information
-
the enzyme consists of a catalytic RNA component and nine essential proteins, RNA-protein UV crosslinking studies for structure analysis, comparison to yeast RNase MRP, overview. 3D Mapping of RNA-protein interactions
additional information
-
8-component RNase P (RNA plus proteins Pop1, Pop4, Pop5, Pop6, Pop7, Pop8, Rpp1). Protein Pop1 is required for the catalytic RNA activation and is positioned to provide a major contribution to its global fold, and, simultaneously, to potentially contribute to both substrate binding and the organization of the catalytic core. Proteins Pop6, Pop7 appear to be structural subunits that, together with the specialized RNA domain P3, form an interface for the Pop1 binding, while Pop8 is required for the proper interactions between Pop1 and proteins shared with the archaeal enzymes, Rpp1/Pop5. Proteins Pop6, Pop7, and Pop8 do not affect the position of the pre-tRNA substrate cleavage site, but increase the activity and stability of the RNP. Proteins Rpp1, Pop5 are required for RNA activation, and bind in the immediate vicinity of the RNA based catalytic core. In addition, Rpp1, Pop5 affect the specificity domain of yeast RNase P RNA, and are required for the engagement of Pop4. Pop4 binding affects a phylogenetically conserved part of RNase PRNA that is directly involved in substrate recognition in bacteria, and increases the level of RNase P activity. Pop4 does not affect the location of the cleavage site in the pre-tRNA substrate and is not absolutely required for the activation of the catalytic RNA
additional information
-
the enzyme consists of a catalytic RNA component and nine essential proteins, RNA-protein UV crosslinking studies for structure analysis, comparison to yeast RNase MRP, overview. 3D Mapping of RNA-protein interactions
-
additional information
-
protein subunit structure, the enzyme folds as an alpha-beta sandwich and has the overall topology of alpha(beta)3alphabetaalpha, overview
additional information
-
active holoenzymes can be reconstituted from the Thermotoga aquaticus and the Thermotoga maritima RNAs and the protein component of RNase P from Escherichia coli
additional information
wild-type and mutant enzyme structure-function analysis, overview
additional information
-
wild-type and mutant enzyme structure-function analysis, overview
additional information
-
active holoenzymes can be reconstituted from the Thermotoga aquaticus and the Thermotoga maritima RNAs and the protein component of RNase P from Escherichia coli
additional information
-
the enzyme contains an extremely large RNase P RNA subunit, about 1100 nt long
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D138A
inactive mutant enzyme
D142A
inactive mutant enzyme
D144A
the mutant enzyme is completely active
D160A
inactive mutant enzyme
C344A
site-directed mutagenesis, the mutant shows a 19% reduced zinc level compared to the wild-type enzyme
C347A
site-directed mutagenesis, the mutant shows a 29% reduced zinc level compared to the wild-type enzyme
C565A
site-directed mutagenesis, the mutant shows a 75% reduced zinc level compared to the wild-type enzyme
C56A
site-directed mutagenesis, the mutant shows no enzyme activity
C56G
site-directed mutagenesis, the mutant shows no enzyme activity
C57A
site-directed mutagenesis, the mutant shows 90% of wild-type enzyme activity
C57C
site-directed mutagenesis, the mutant shows 10% of wild-type enzyme activity
D399A
mutation significantly reduces activity. No product formation is observed after a 30-min incubation under standard STO assay conditions (1 mM MgCl2). No increase in activity, when Mg2+ concentration increases from 1 mM to 20 mM
D474A
mutation significantly reduces activity. No product formation is observed after a 30-min incubation under standard STO assay conditions (1 mM MgCl2). Activity increases significantly at the 20 mM Mg2+ compared to 1 mM Mg2+
D474A/D475A
site-directed mutagenesis, the mutant shows 3,3% reduction of the zinc level compared to the wild-type enzyme
D475A
mutation significantly reduces activity. No product formation is observed after a 30-min incubation under standard STO assay conditions (1 mM MgCl2). Activity increases significantly at the 20 mM Mg2+ compared to 1 mM Mg2+
D493A
mutation significantly reduces activity. No product formation is observed after a 30-min incubation under standard STO assay conditions (1 mM MgCl2). No increase in activity, when Mg2+ concentration increases from 1 mM to 20 mM
G18A
site-directed mutagenesis, the mutant shows 15% of wild-type enzyme activity
G18C
site-directed mutagenesis, the mutant shows 10% of wild-type enzyme activity
G19A
site-directed mutagenesis, the mutant shows 85% of wild-type enzyme activity
G19C
site-directed mutagenesis, the mutant shows 90% of wild-type enzyme activity
H548A
site-directed mutagenesis, the mutant shows a 60% reduced zinc level compared to the wild-type enzyme
E40C
-
site-directed mutagenesis, comparison of metal effects on enzyme-substrate complex formation with the wild-type enzyme
F16A
-
affinity of RNase P for A(-4) pre-tRNA is decreased more than 10fold
F16C
-
increases the affinity for G(-4) pre-tRNA by at least 25fold
F20A
-
decrease in the affinity of A(-4) pre-tRNA compared to that of G(-4) pre-tRNA, causing the A(-4)/G(-4) selectivity ratio to decrease to less than 1. Mutations in the central cleft of P protein alters the observed cleavage rate constant by less than 2fold
K64A
-
affinity of RNase P for A(-4) pre-tRNA is decreased
N61A
-
affinity of RNase P for A(-4) pre-tRNA is decreased
Y113C
-
site-directed mutagenesis, comparison of metal effects on enzyme-substrate complex formation with the wild-type enzyme
Y34A
-
decrease in the affinity of A(-4) pre-tRNA compared to that of G(-4) pre-tRNA, causing the A(-4)/G(-4) selectivity ratio to decrease to less than 1. Mutations in the central cleft of P protein alters the observed cleavage rate constant by less than 2fold
Y34F
-
decreases A(-4) pre-tRNA binding affinity, although to a smaller extent than mutant Y34A. Binds A(-4) and P(-4) pre-tRNAs with comparable affinities. Mutations in the central cleft of P protein alters the observed cleavage rate constant by less than 2fold
A333C
-
no effect on activity of M1 RNA on wild-type Escherichia coli SuIII tRNATyr precursor
A334U
-
much lower activity on activity of M1 RNA on wild-type Escherichia coli SuIII tRNATyr precursor
G224A/G225A
-
ribozymes carrying the mutation at the catalytic RNA exhibit at least 10times higher cleavage efficiency than the wild-type enzyme
N32A/E33A/K36A
mutant protein L7Ae displays only 4% of the activity observed with the wild-type protein L7Ae
H67A
spectrum of mutant is moderately altered at 37°C, indicative of subtle structural changes arising due to the mutation. The H67A protein shows significant loss in secondary structure at 45°C, which further enhances at 55°C. The loss of structure with increase in temperature is relatively less in the case of wild-type and H67N proteins. kcat/Km-value is 1.9fold lower than the value for the wild-type enzyme
H67N
spectrum of mutant is moderately altered at 37°C, indicative of subtle structural changes arising due to the mutation. The H67A protein shows significant loss in secondary structure at 45°C, which further enhances at 55°C. The loss of structure with increase in temperature is relatively less in the case of wild-type and H67N proteins. kcat/Km-value is 1.4fold lower than the value for the wild-type enzyme
H67A
-
spectrum of mutant is moderately altered at 37°C, indicative of subtle structural changes arising due to the mutation. The H67A protein shows significant loss in secondary structure at 45°C, which further enhances at 55°C. The loss of structure with increase in temperature is relatively less in the case of wild-type and H67N proteins. kcat/Km-value is 1.9fold lower than the value for the wild-type enzyme
-
H67N
-
spectrum of mutant is moderately altered at 37°C, indicative of subtle structural changes arising due to the mutation. The H67A protein shows significant loss in secondary structure at 45°C, which further enhances at 55°C. The loss of structure with increase in temperature is relatively less in the case of wild-type and H67N proteins. kcat/Km-value is 1.4fold lower than the value for the wild-type enzyme
-
A14V
-
RPP21 mutant, wild-type RPP21 binds to RPP29 3fold tighter than the mutant
C71V
-
the single-Cys substitutions are introduced into a Cys-less Pfu L7Ae template C71V (i.e. RNA-binding protein L7Ae, subunit of archaeal RNase P). The native C71, which is partly buried, is mutated to Val to preserve the native fold and hydrophobic core of the protein. The C71V parental reference is more active than the wild type enzyme
K42C
-
mutation does not affect activity. The single-Cys substitution is introduced into a Cys-less Pfu L7Ae template C71V (i.e. RNA-binding protein L7Ae, subunit of archaeal RNase P). The native C71, which is partly buried, is mutated to Val to preserve the native fold and hydrophobic core of the protein
R46C
-
mutation results in 28% decrease in activity. The single-Cys substitution is introduced into a Cys-less Pfu L7Ae template C71V (i.e. RNA-binding protein L7Ae, subunit of archaeal RNase P). The native C71, which is partly buried, is mutated to Val to preserve the native fold and hydrophobic core of the protein
V95C
-
mutation results in 6% decrease in activity. The single-Cys substitution is introduced into a Cys-less Pfu L7Ae template C71V (i.e. RNA-binding protein L7Ae, subunit of archaeal RNase P). The native C71, which is partly buried, is mutated to Val to preserve the native fold and hydrophobic core of the protein
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
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
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
E47A
mutant shows activity similar to the wild type enzyme
E73A
mutant shows reduced activity compared to the wild type enzyme
F95A
mutant shows reduced activity compared to the wild type enzyme
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
K121A
mutant shows activity similar to the wild type enzyme
K122A
mutant shows activity similar to the wild type enzyme
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
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
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
R115A
mutant shows reduced activity compared to the wild type enzyme
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
R75A
mutant shows reduced activity compared to the wild type enzyme
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
-
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
-
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
-
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
-
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
-
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
-
R233K
-
temperature-sensitive POP1 mutant
R626L/P628K
-
temperature-sensitive POP1 mutant
A347C/C348U/C353G/C354GC355AG356U
-
M1-C2, is derived from M1-C1 by introducing several point mutations at the catalytic P4 domain. Is catalytically inactive
G190U/A258C
-
functional ribozyme M1-C1, the 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, which yields efficient cleavage
F17A
site-directed mutagenesis of the protein part, the mutant shows 95% reduced activity compared to the wild-type enzyme
F17A/U52C
site-directed mutagenesis of the protein part (F17A) and the RNA part (U52C), the mutant shows over 99% reduced activity compared to the wild-type enzyme
F21A
site-directed mutagenesis of the protein part, the mutant shows 80% reduced activity compared to the wild-type enzyme
K51A
site-directed mutagenesis of the protein part, the mutant shows 60% reduced activity compared to the wild-type enzyme
K53A
site-directed mutagenesis of the protein part, the mutant shows 80% reduced activity compared to the wild-type enzyme
K56A
site-directed mutagenesis of the protein part, the mutant shows 10% increased activity compared to the wild-type enzyme
K62A
site-directed mutagenesis of the protein part, the mutant shows unaltered activity compared to the wild-type enzyme
K90A
site-directed mutagenesis of the protein part, the mutant shows 70% reduced activity compared to the wild-type enzyme
R14A
site-directed mutagenesis of the protein part, the mutant shows 60% reduced activity compared to the wild-type enzyme
R15A
site-directed mutagenesis of the protein part, the mutant shows 70% reduced activity compared to the wild-type enzyme
R52A
site-directed mutagenesis of the protein part, the mutant shows 60% reduced activity compared to the wild-type enzyme
R59A
site-directed mutagenesis of the protein part, the mutant shows 20% increased activity compared to the wild-type enzyme
R60A
site-directed mutagenesis of the protein part, the mutant shows 30% reduced activity compared to the wild-type enzyme
R65A
site-directed mutagenesis of the protein part, the mutant shows 50% increased activity compared to the wild-type enzyme
R89A
site-directed mutagenesis of the protein part, the mutant shows 94% reduced activity compared to the wild-type enzyme
R89A/U52C
site-directed mutagenesis of the protein part (R89A) and the RNA part (U52C), the mutant shows over 99% reduced activity compared to the wild-type enzyme
U52C
site-directed mutagenesis of the RNA part, the mutant shows 92% reduced activity compared to the wild-type enzyme
K64C
-
site-directed mutagenesis of the RNR motif of P protein subunit, the mutant shows unaltered RNA binding kinetics compared to the wild-type enzyme
K64C
-
site-directed mutagenesis of an RNR motif residue, the mutant shows altered binding affinity for the substrate and between its components compared to the wild-type enzyme
R60A
-
decrease in the affinity of A(-4) pre-tRNA compared to that of G(-4) pre-tRNA, causing the A(-4)/G(-4) selectivity ratio to decrease to less than 1
R60A
-
site-directed mutagenesis of the RNR motif of P protein subunit, the mutant shows unaltered RNA binding kinetics compared to the wild-type enzyme
R60A
-
site-directed mutagenesis of an RNR motif residue, the mutant shows altered binding affinity for the substrate and between its components compared to the wild-type enzyme
R62A
-
site-directed mutagenesis of the RNR motif of P protein subunit, the mutant shows unaltered RNA binding kinetics compared to the wild-type enzyme
R62A
-
site-directed mutagenesis of an RNR motif residue, the mutant shows altered binding affinity for the substrate and between its components compared to the wild-type enzyme
R65A
-
affinity of RNase P for A(-4) pre-tRNA is decreased more than 10fold
R65A
-
site-directed mutagenesis of the RNR motif of P protein subunit, the mutant shows unaltered RNA binding kinetics compared to the wild-type enzyme
R65A
-
site-directed mutagenesis of an RNR motif residue, the mutant shows altered binding affinity for the substrate and between its components compared to the wild-type enzyme
R65C
-
site-directed mutagenesis of the RNR motif of P protein subunit, the mutant shows unaltered RNA binding kinetics compared to the wild-type enzyme
R65C
-
site-directed mutagenesis of an RNR motif residue, the mutant shows altered binding affinity for the substrate and between its components compared to the wild-type enzyme
R68A
-
site-directed mutagenesis of the RNR motif of P protein subunit, the mutant shows unaltered RNA binding kinetics compared to the wild-type enzyme
R68A
-
site-directed mutagenesis of an RNR motif residue, the mutant shows altered binding affinity for the substrate and between its components compared to the wild-type enzyme
R68C
-
site-directed mutagenesis of the RNR motif of P protein subunit, the mutant shows unaltered RNA binding kinetics compared to the wild-type enzyme
R68C
-
site-directed mutagenesis of an RNR motif residue, the mutant shows altered binding affinity for the substrate and between its components compared to the wild-type enzyme
additional information
-
construction of mutant enzyme chimeras consisting of either Escherichia coli protein components and Bacillus subtilis RNA component or vice versa
additional information
-
mutagenesis of the CR-IV region of the enzyme RPR1 RNA results in large reduction of kcat with little effect on Km
additional information
-
RNR motif mutations do not alter the kinetics of pre-tRNA cleavage
additional information
-
L5.1-L15.1 intradomain contact in the catalytic domain of the prototypic type B RNase P RNA of Bacillus subtilis is crucial for adopting a compact functional conformation. Disruption of the L5.1-L15.1 contact by antisense oligonucleotides or mutation reduces P RNA-alone and holoenzyme activity by one to two orders of magnitude in vitro, largely retards gel mobility of the RNA and further affects the structure of regions P7/P8/P10.1, P15 and L15.2, and abolishes the ability of Bacillus subtilis P RNA to complement a P RNA-deficient Escherichia coli strain
additional information
-
construction of mutants inactive with pre-4.5S RNA but not with pre-tRNA
additional information
-
construction of deletion mutants of subunit DRpp29, analysis of interaction of the mutants with RNase P subunit compared to the wild-type subunit DRpp29 and compared to the modeling data, overview
additional information
-
construction of deletion mutants of subunit DRpp29, analysis of interaction of the mutants with RNase P subunit compared to the wild-type subunit DRpp29 and compared to the modeling data, overview
-
additional information
-
temperature-sensitive mutant that is defective in RNase P activity carries a mutant gene that has GC-AT substitutions at positions corresponding to 89 and 365 nucleotides downstream from the 5' terminus of the RNA sequence. Comparing to the wild-type RNA, the mutant RNA is less stable and rapidly degraded in vivo and vitro
additional information
-
RNase P activity can be detected with holoenzymes reconstituted with the RNA subunit from Escherichia coli and the protein subunit from Synechocystis 6803 or with the RNA subunit from Synechocystis 6803 and the protein subunit from Escherichia coli
additional information
-
ribozyme variant O67 contains a deletion of G336 and mutations of G224G225/A224A225, G230/C230 and A337G and exhibits 20fold higher activity to cleave the TK mRNA sequence than the wild-type ribozyme under both high and low concentrations of Mg2+ ions
additional information
-
binding and catalysis of J5/15 and N(-1) mutants, overview, mutation of the A248 nucleotide results in defects in thermodynamics and in miscleavage of substrates containing 2'deoxy modification at N(-1), compensatory mutation of N(-1) restore correct cleavage activity in reaction with both, the RNA subunit alone and the holoenzyme, influence of nucleotide at position N(-2)
additional information
-
construction of mutant enzyme chimeras consisting of either Escherichia coli protein components and Bacillus subtilis RNA component or vice versa
additional information
-
mutagenesis of the CR-IV region of the enzyme RPR1 RNA results in large reduction of kcat with little effect on Km
additional information
-
the use of Ca2+ as catalytic metal ion is enhanced in nucleotide point mutants C70U and U69 deletion in the P4 helix
additional information
-
change of RNase P RNA function by single base mutation correlates with perturbation of metal ion binding in P4
additional information
-
examining the bases of the J3/4 domain of Escherichia coli ribonuclease P. Replacement, deletion, or insertion, except at G63G64, can be compensated for the presence of a high concentration of magnesium ions above 20 mM
additional information
-
variant with a point mutation at nucleotide 95 of RNaseP catalytic RNA G95U that increases the rate of cleavage, and another mutation at A200C that enhances substrate binding of the ribozyme
additional information
-
construction of a mutant variant M1GS ribozyme via combined mutations at nucleotide 83 and 340 of RNase P catalytic RNA (G83 -. U83 and G340 -. A340). The mutant ribozyme shows an increase in overall efficiency in cleaving an HIV RNA sequence compared to the wild-type enzyme
additional information
-
construction of a rnpA knockout strain (MTea1), deletion of the essential endogenous rnpA copy and simultaneous replacement by a heterologous version of the gene, i.e. by eight rnpA sequences from Proteus mirabilis, Pseudomonas aeruginosa, Acinetobacter baumannii, Neisseria gonorrhoaea, Bacillus subtilis, Streptococcus oralis, Staphylococcus aureus, and Thermotoga maritima. The increasingly divergent versions of the RNase P protein all complement the loss of the endogenous rnpA gene, phylogenetic range of rnpA heterologues, overview
additional information
-
construction of the enzyme-deficient rnpA49 rph-1 mutant strain. Increased levels of the M1 RNA, the enzyme's rNA subunit, partially complement the rnpA49 allele at 42°C. Simultaneous expression of tRNAval(GAC) and tRNAval(UAC) does not suppress the temperature sensitivity of the rnpA49 strain. In contrast, overproduction of the rnpB gene leads to a small improvement in the growth of the rnpA49 rph-1 strain at 42°C
additional information
-
seperation of the catalytic domain of the RNA part by cleaving it from the specificity S-domain mediates. Compared to full-length RNase P RNA, the rate constant, kobs, of cleavage of various model RNA hairpin loop substrates.for the truncated RPR is reduced 30 to 13000fold depending on the substrate. Substitution of A248, positioned near the cleavage site in the RNase P-substrate complex, with G in the truncated RNase P RNA results in 30fold improvement in reaction rate. In contrast, strengthening the interaction between the RNase P RNA and the 3'-end of the substrate only had a modest effect. Deleting the S-domain gives a reduction in the rate, but it results in a less erroneous RPR with respect to cleavage site selection
additional information
-
construction of the enzyme-deficient rnpA49 rph-1 mutant strain. Increased levels of the M1 RNA, the enzyme's rNA subunit, partially complement the rnpA49 allele at 42°C. Simultaneous expression of tRNAval(GAC) and tRNAval(UAC) does not suppress the temperature sensitivity of the rnpA49 strain. In contrast, overproduction of the rnpB gene leads to a small improvement in the growth of the rnpA49 rph-1 strain at 42°C
-
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
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
-
additional information
-
complete deletion of the protein subunit is lethal, mutation of P3 loop causes defects in pre-tRNA processing and enzyme RPR1 RNA maturation as well as subunit interaction in vivo
additional information
-
construction of a pre-tRNA substrate in which the pro-Rp nonbridging oxygen of the scissile bond is replaced by sulfur
additional information
-
mutations in yeast RPR1 RNA at the loop regions of eP8 hairpin (eP8m), eP9 hairpin (eP9m), the junction of P4/P7 (jP4/7m), and the junction of P7/eP15 (jP7/15m). The mutation of jP7/15m does not affect cell growth, tRNA processing, or RNase P maturation. Mutants in eP8m, eP9m, and jP4/7m display pronounced growt defects and pre-tRNA processing defects in vivo
additional information
-
Trypanosoma brucei proteinaceous enzyme PRORP1 can substitute for yeast nuclear RNase P in vivo
additional information
-
construction of a functional RNase P-based ribozyme, M1GS RNA, that targets the overlapping mRNA region of M80.5 and protease, two murine cytomegalovirus proteins essential for viral replication. Construction of an attenuated strain of Salmonella, which exhibits efficient gene transfer activity and little cytotoxicity and pathogenicity in mice, for delivery of anti-MCMV ribozyme. In MCMV-infected macrophages treated with the constructed attenuated Salmonella strain carrying the functional M1GS RNA construct, a 80-85% reduction in the expression of M80.5/protease and a 2500fold reduction in viral growth is observed. The strain delivers efficiently delivered antiviral M1GS RNA into spleens and livers, leading to substantial expression of the ribozyme without causing significant adverse effects in the animals. MCMV-infected mice treated orally with Salmonella carrying the functional M1GS sequence display reduced viral gene expression, decreased viral titers, and improved survival compared to the untreated mice or mice treated with Salmonella containing control ribozyme sequences
additional information
-
RNase P activity can be detected with holoenzymes reconstituted with the RNA subunit from Escherichia coli and the protein subunit from Synechocystis 6803 or with the RNA subunit from Synechocystis 6803 and the protein subunit from Escherichia coli
additional information
wild-type and mutant enzyme structure-function analysis, overview. Point mutations in the conserved protein loop (residues 52-57) have either no or modest effects on catalytic efficiency. Similarly, amino acid changes in the RNR region, which represent the most conserved region of bacterial RNase P proteins, exhibit negligible changes in catalytic efficiency
additional information
-
wild-type and mutant enzyme structure-function analysis, overview. Point mutations in the conserved protein loop (residues 52-57) have either no or modest effects on catalytic efficiency. Similarly, amino acid changes in the RNR region, which represent the most conserved region of bacterial RNase P proteins, exhibit negligible changes in catalytic efficiency
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