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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

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 Hydrolases
         3.1 Acting on ester bonds
             3.1.26 Endoribonucleases producing 5'-phosphomonoesters
                3.1.26.5 ribonuclease P

Purification

Purification on EC 3.1.26.5 - ribonuclease P

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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity purification
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affinity purified
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by Ni-NTA affinity chromatography
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copurified with nuclear RNAs by aptamer-streptavidin affinity chromatography and TAP column chromatography
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DEAE-Sepharose column chromatography and Sephacryl S-100 gel filtration
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HiTrap column chromatography and C4 reversed-phase high performance liquid chromatography
mitochondrial enzyme, and RNase P partially
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MRPP1, affinity purified
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native nuclear enzyme partially purified from leaves employing anion exchange chromatography, and from floral buds employing two different steps of anion exchange chromatography, ammonium sulfate fractionation, and gel filtration, purification of recombinant His6-tagged proteins StPop5 and StRpp25 from Escherichia coli strain BL21(DE3)
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Ni-NTA column chromatography
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nuclear enzyme
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P protein purified by ion exchange chromatography under denaturing conditions
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partial
partial purification into protein and RNA subunit. Reconstitution of homologous enzyme complex and heterologous enzyme complexes with subunits from the Escherichia coli enzyme
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partial. The RNase P RNA lacks essential secondary structures required for the recognition of pre-tRNA and as a result is not catalytically active in vitro
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partially
partially from 800-900fold over the chloroplast lysate
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partially purified
partially purified by DEAE Sepharose column chromatography
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partially purified by ion-exchange chromatography
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partially, 2400fold
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phosphocellulose column chromatography
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protein component
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protein moiety. Reconstitution of the holoenzyme when mixed with M1 RNA
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purification and report of a stepwise reconstitution of 8-component RNase P (RNA plus proteins Pop1, Pop4, Pop5, Pop6, Pop7, Pop8, Rpp1)
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purification of the recombinant protein and RNA components and reconstitution of the holoenzyme in vitro
purified to homogeneity by using cation-exchange and reversed-phase chromatography
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Q sepharose column chromatography
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recombinant C-terminally His6-tagged PRORP1 from Escherichia coli by nickel affinity chromatography, recombinant C-terminally His6-tagged and N-terminally GST-tagged PRORP2 from Escherichia coli by nickel and glutathione affinity chromatography, and proteolytical cleavage of the GST-tag, both proteins ar further purified by gel filtration
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recombinant enzyme
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recombinant enzyme from Escherichia coli strain BL21(DE3) by cation exchange and metal chelating affinity chromatography
recombinant enzyme from Escherichia coli strain Rosetta (DE3)pLysS by nickel affinity chromatography
L0N807
recombinant GST-tagged wild-type and mutant proteins and RNA from Escherichia coli strain BL21(DE3)pLysS
recombinant His-tagged subunits Rpp14, Rpp20, Rpp21, Rpp25, Rpp29, Rpp30, Rpp38, Rpp40, and hPop5 from Escherichia coli as soluble and refolded proteins
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recombinant protein and RNA subunits H1, Rpp21, and Rpp29 from Escherichia coli
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recombinant protein subunit from Escherichia coli, to homogeneity
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recombinant protein subunit Rpp25, and native wild-type enzyme from HeLa cells
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recombinant untagged and His-tagged enzymes
recombinant wild-type and mutant protein subunits from Escherichia coli
ribonuclease P protein components 1, 2, 3 and 4 are expressed in Escherichia coli cells, and the resulting proteins Ph1481p, Ph1601p, Ph1771p, and Ph1877p are purified to apparent homogeneity in a set of column chromatographies. RNase P reconstituted of four proteins with the in vitro transcripted Pyrococcus horikoshii RNase P RNA exhibits enzymatic properties like those of native enzyme
RNA moiety
RNA subunit, partial
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RNase P from nucleus
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RNase P from Sulfolubus solfataricus is purified 800fold by Trisacryl-DEAE, and Sepharose CL-6B chromatographies and Cs2S04 buoyant density centrifugation
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RPP21 and RPP29. RPP29 eluted and ultrafiltrated
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SP-Sepharose column chromatography
tandem affinity chromatography
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tandem affinity purification tag chromatography, calmodulin affinity resin chromatography, and DEAE Sepharose column chromatography
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to homogeneity
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