3.1.26.5: ribonuclease P
This is an abbreviated version!
For detailed information about ribonuclease P, go to the full flat file.
Word Map on EC 3.1.26.5
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3.1.26.5
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ribonucleoproteins
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pre-trnas
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endoribonuclease
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endonucleolytic
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eculizumab
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aminoacylation
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rna-based
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stem-loops
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phosphodiester
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nucleolar
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nocturnal
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eubacterial
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paroxysmal
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gene-targeting
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anticodon
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base-pairing
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rna-protein
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sars-cov-2
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c5a
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horikoshii
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hemoglobinuria
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trna-like
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pyrococcus
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swab
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3'-terminal
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5\'-leader
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riboswitches
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trnatyr
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2'-hydroxyls
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trnahis
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trailer
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cloverleaf
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rna-rna
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self-splicing
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protein-rna
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tmrna
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micrococcal
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self-cleaving
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t-loops
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p-mediated
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complement-mediated
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ncrnas
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pseudoknots
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watson-crick
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eukaryal
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oligoribonucleotides
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analysis
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pharmacology
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snornps
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synthesis
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medicine
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biotechnology
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trnase
- 3.1.26.5
- ribonucleoproteins
- pre-trnas
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endoribonuclease
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endonucleolytic
- eculizumab
- aminoacylation
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rna-based
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stem-loops
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phosphodiester
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nucleolar
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nocturnal
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eubacterial
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paroxysmal
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gene-targeting
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anticodon
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base-pairing
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rna-protein
- sars-cov-2
- c5a
- horikoshii
- hemoglobinuria
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trna-like
- pyrococcus
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swab
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3'-terminal
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5\'-leader
- riboswitches
- trnatyr
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2'-hydroxyls
- trnahis
- trailer
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cloverleaf
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rna-rna
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self-splicing
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protein-rna
- tmrna
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micrococcal
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self-cleaving
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t-loops
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p-mediated
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complement-mediated
- ncrnas
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pseudoknots
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watson-crick
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eukaryal
- oligoribonucleotides
- analysis
- pharmacology
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snornps
- synthesis
- medicine
- biotechnology
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trnase
Reaction
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor =
Synonyms
Aq_880, aRpp29, aRpp29 protein, AtPop1p, AtPRORP1, AtPRORP2, AtPRORP3, C5 protein, CrPRORP, hPOP1, hPOP4, hPOP7, M1 RNA, M1GS, M1GS RNA, mitochondrial RNase P protein 1, MRPP1, MRPP2, MRPP3, nuclear ribonclease P ribonucleoprotein, nuclease, ribo-, P, Pfu Pop5, PhoPRNA, POP1, Pop1p, Pop5, Pop6, Pop7, PRORP, PRORP1, PRORP2, PRORP3, Protein C5, protein-only ribonuclease P, protein-only RNase P, protein-only RNase P enzyme, proteinaceous RNase P, ribonuclease MRP, ribonuclease P, ribonuclease P ribozyme, ribosomal RNA processing ribonucleoprotein, Ribunuclease P, RNA processing protein POP1, RNA processing protein POP5, RNA processing protein POP6, RNA processing protein POP7, RNA processing protein POP8, RNase MRP, RNase P, RNase P holoenzyme, RNase P protein, RNase P ribozyme, RNase P RNA, RNase P/MRP, RNase P/MRP protein, RNaseP protein, RNaseP protein p20, RNaseP protein p30, RNaseP protein p38, RNaseP protein p40, RNases P, RNP, Rpm2p, RPP, RPP14, Rpp20, Rpp21, Rpp25, Rpp29, Rpp30, Rpp38, RPP40, RPR, RPR1, transfer RNA 5' maturation enzyme, transfer RNA processing enzyme, tRNA processing enzyme, tRNA-processing endonuclease, tRNA-processing enzyme
ECTree
3.1.26.5 ribonuclease PAdvanced search results
results (
results (Subunits
Subunits on EC 3.1.26.5 - ribonuclease P
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
decamer
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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
dimer
homodimer
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2 * 16000, full-length Rpp20, gel filtration. 2 * 14100, Rpp20(16-140), gel filtration. 2 * 13200, HisRpp20(35-140), gel filtration
octamer
oligomer
tetramer
ribonuclease P protein component 1 (PH1771), ribonuclease P protein component 2 (PH1481), ribonuclease P protein component 3 (PH1877), ribonuclease P protein component 4 (PH1601). Three proteins Ph1481p, Ph1601p, and Ph1771p, and RNase P RNA are minimal components for the RNase P activity. However, addition of the fourth protein Ph1877p strongly stimulated enzymatic activity, indicating that all four proteins and RNase P RNA are essential for optimal RNase P activity
additional information
?
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+
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x * 100000, SDS-PAGE
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?
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x * 18000, recombinant His6-tagged protein StPop5, SDS-PAGE, x * 33000, recombinant His6-tagged protein StRpp25, SDS-PAGE
dimer
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x * 13990-14000, protein subunit, + x * ?, RNA subunit, SDS-PAGE and mass spectrometry
dimer
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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
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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
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octamer
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1 * 19000, + 1 * 21000, + 1 * 30000, + 1 * 33000, + 1 * 45000, + 1 * 85000, + 1 * 125000, polypeptides, + 1 * ?, RNA component, SDS-PAGE
octamer
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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enzyme secondary structure and tertiary interactions, overview
additional information
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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
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the mitochondrial enzyme contains an RNA subunit and 7 protein subunits of 16-55 kDa
additional information
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RNA and protein subunits from one species can complement subunits from the other species in reconstitution experiments
additional information
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the protein component both alters the conformation of the RNA component and enhances the substrate affinity and specificity
additional information
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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
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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
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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
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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
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subunit composition, 1 large RNA subunit plus 1 small protein subunit contributing to about 10% of the mass of the holoenzyme
additional information
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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
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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
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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
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enzyme secondary structure and tertiary interactions, overview
additional information
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ribonuclease P is composed of a catalytically active RNA (PRNA) and a small protein (P protein) subunit
additional information
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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
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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
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additional information
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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
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RNA and protein subunits from one species can complement subunits from the other species in reconstitution experiments
additional information
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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
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enzyme is composed of a large RNA subunit of about 400 nucleotides and a smaller protein subunit
additional information
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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
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enzyme secondary structure, domain organization and tertiary structure, modeling, overview
additional information
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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
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subunit composition, 1 large RNA subunit plus 1 small protein subunit contributing to about 10% of the mass of the holoenzyme
additional information
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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
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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
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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
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enzyme secondary structure and tertiary interactions, overview
additional information
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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
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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
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the essential enzyme consists of the C5 protein and the catalytic M1 RNA subunits
additional information
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the essential enzyme consists of the C5 protein and the catalytic M1 RNA subunits
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additional information
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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
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autoantigenic properties of the protein subunits Rpp38 and Rpp30 of catalytically active complexes of human ribonuclease P
additional information
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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
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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
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subunit composition, secondary structure of the enzyme RNA moiety
additional information
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subunit composition, at least 4 protein subunits namely MTH11, MTH687, MTH688, and MTH1618
additional information
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subunit composition, secondary structure of the enzyme RNA moiety
additional information
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RNase P contains an essential RNase P RNA and RNase P protein
additional information
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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
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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
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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
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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
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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
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additional information
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enzyme is a ribonucleoprotein consisting of multiple protein components and a single RNA species
additional information
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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
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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
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the mitochondrial enzyme contains a single RNa subunit and a single protein subunit
additional information
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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
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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
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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
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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
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additional information
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protein subunit structure, the enzyme folds as an alpha-beta sandwich and has the overall topology of alpha(beta)3alphabetaalpha, overview
additional information
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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
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wild-type and mutant enzyme structure-function analysis, overview
additional information
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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
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the enzyme contains an extremely large RNase P RNA subunit, about 1100 nt long
