3.1.26.5: ribonuclease P
This is an abbreviated version!
For detailed information about ribonuclease P, go to the full flat file.
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
Application
Application on EC 3.1.26.5 - ribonuclease P
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
magnetic sensor technique suitable for the measurement of specific RNA-protein interactions, whereby properties of the streptavidin-coated magnetic beads decide on success or failure of the technique
analysis
-
potential for using RNase P ribozymes as gene-targeting agents against any mRNA sequences, and using the selection procedure and a general approach for the engineering of RNase P ribozymes
analysis
-
coupling DNA micro-arrays with conditional mutants of RNase P in yeast is a powerful approach to conduct genomewide searches and identify new substrates (e.g., polycistronic mRNAs, snoRNAs)
analysis
-
fluorescein labeling has only a modest effect on the binding affinity of pre-tRNA and this fluorescent titration method may be useful for rapidly measuring the affinity of RNase P for a wide variety of substrates
biotechnology
-
RNA-mediated RNA cleavage events are being increasingly exploited to disrupt RNA function, an important objective in post-genomic biology. RNase P, a ribonucleoprotein enzyme that catalyzes the removal of 5'-leaders from precursor tRNAs, has previously been utilized for sequence-specific cleavage of cellular RNAs
biotechnology
-
RNA-mediated RNA cleavage events are being increasingly exploited to disrupt RNA function, an important objective in post-genomic biology. RNase P, a ribonucleoprotein enzyme that catalyzes the removal of 5'-leaders from precursor tRNAs, has previously been utilized for sequence-specific cleavage of cellular RNAs
biotechnology
-
RNA-mediated RNA cleavage events are being increasingly exploited to disrupt RNA function, an important objective in post-genomic biology. RNase P, a ribonucleoprotein enzyme that catalyzes the removal of 5'-leaders from precursor tRNAs, has previously been utilized for sequence-specific cleavage of cellular RNAs
biotechnology
-
RNA-mediated RNA cleavage events are being increasingly exploited to disrupt RNA function, an important objective in post-genomic biology. RNase P, a ribonucleoprotein enzyme that catalyzes the removal of 5'-leaders from precursor tRNAs, has previously been utilized for sequence-specific cleavage of cellular RNAs
biotechnology
-
RNase P of Escherichia coli contains a catalytic RNA subunit (M1 RNA) that can be engineered to cleave tRNA-like substrates and other target RNAs, including specific mRNAs. The enzyme can be expressed in infected human U373MG cells or fibroblasts, or in murine PA317 cells, and therein be used for inhibition of targeting and cleavage of host RNA by Human cytomegalovirus enzyme, HCMV strain AD169, through blocking substrate mRNA expression, methods of using engineered RNase P catalytic RNA for in vitro and in vivo in trans-cleavage of target viral mRNA, overview. customized M1GS RNA and full-length RNase P are effective in cleaving both viral and cellular mRNAs and blocking their expression in cultured cells
medicine
-
catalytic RNase P RNA from Synechocystis sp. may be an active agent for Hepatitis C virus interventions
medicine
-
RNase P ribozyme 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) is highly effective in inhibiting herpes simplex virus 1 gene expression
medicine
-
RNase P RNA is a drug target for aminoglycoside-arginine conjugates
medicine
-
ability to purify large amounts of M1 RNA, 20fold greater level from transformed cells than that from untransformed cells. M1GSs (tethered to the 3' end of M1 RNA by a spacer of 20-50 nt is a guide sequence (13-16 nt) that base pairs with the target RNA and has an unpaired 3'-RCCA needed for interacting with M1 RNA) degrades the oncogenic chimera BCR-ABL mRNA specifically and halted cancer development in mammalian cells when the guide sequence is designed to target the fusion region
medicine
-
feasibility to develop Salmonella-mediated gene transfer of RNase P ribozymes as an effective approach for gene-targeting applications
medicine
-
RNase P technology is a potential antiviral agent. Advantage of the external guide sequences technology over the M1GSs technology in therapy is the use of the endogenous RNase P enzyme and external guide sequences are much shorter than M1GSs. Advantage of random external guide sequences technique is that it will identify target sites that are accessible for binding of an antisense oligo and at the same time identify if these target sites are suitable substrates for cleavage by RNase P holoenzyme. M1GS technology works efficiently in inhibition of viral pathogenesis in immunodeficient mice
medicine
Acinetobacter baumannii is a problematic pathogen that is commonly resistant to multiple antibiotics. The RNase P endonucleolytic activity is characterized by having structural but not sequence substrate requirements. This property leads to development of EGS technology, which consists of utilizing a short antisense oligonucleotide that when forming a duplex with a target RNA induces its cleavage by RNase P. External guide sequence (EGS) technology can be a viable option for designing therapeutic alternatives to treat multiresistant Acinetobacter baumannii infections
medicine
construction of external guide sequences (EGSs) from a variant to target the mRNA encoding herpes simplex virus 1 (HSV-1) major transcription regulator ICP4, which is essential for the expression of viral early and late genes and viral growth. The EGS variant induces human RNase P cleavage of ICP4 mRNA sequence 60times better than the EGS generated from a natural pre-tRNA. A decrease of about 97% and 75% in the level of ICP4 gene expression and an inhibition of about 7,000- and 500-fold in viral growth are observed in HSV infected cells expressing the variant and the pre-tRNA-derived EGS, respectively. The study shows that engineered external guide sequences (EGSs) can inhibit HSV-1 gene expression and viral growth. The results demonstrate the potential for engineered EGS RNAs to be developed and used as anti-HSV therapeutics
medicine
-
two different technologies are developed to use RNase P as a tool for RNA knockdown. In one of these, an external guide sequence (EGS), which mimics a tRNA precursor, a well-known natural RNase P substrate, is used to target an RNA molecule for cleavage by endogenous RNase P. Alternatively, a guide sequence can be attached to M1 RNA, the (catalytic) RNase P RNA subunit of Escherichia coli. The guide sequence is specific for an RNA target, which is subsequently cleaved by the bacterial M1 RNA moiety. These approaches are applicable in both bacteria and eukaryotes. The RNase P EGS and M1GS technologies to knockdown specific RNAs are useful strategy in combating infectious diseases. External guide sequence (EGS) and M1 guide sequence (M1GS) successfully reduced bacterial viability, malaria replication and viral infections in cell cultures, and, to a lesser extent, in multicellular organisms. Salmonella-based oral delivery of EGS and M1GS appears to be an attractive way to combat some viral infections in mice and possibly other organisms
medicine
-
Acinetobacter baumannii is a problematic pathogen that is commonly resistant to multiple antibiotics. The RNase P endonucleolytic activity is characterized by having structural but not sequence substrate requirements. This property leads to development of EGS technology, which consists of utilizing a short antisense oligonucleotide that when forming a duplex with a target RNA induces its cleavage by RNase P. External guide sequence (EGS) technology can be a viable option for designing therapeutic alternatives to treat multiresistant Acinetobacter baumannii infections
-
pharmacology
-
specific external guide sequences offer a possibility for specific decrease of gene expression by inhibition of RNase P
pharmacology
-
specific external guide sequences offer a possibility for specific decrease of gene expression by inhibition of RNase P
pharmacology
-
engineered Escherichia coli ribozyme variants are effective in inhibiting HIV infection, the potential of engineering RNase P ribozymes for anti-HIV application
synthesis
-
the bacterial RNase P ribozyme might be used to release RNAs of interest with homogeneous 3'-OH ends from primary transcripts via site-specific cleavage, overview. Also, T7 transcription of mature tRNAs with clustered G residues at the 5'-end may result in 5'-end heterogeneities, which can be avoided by first transcribing the 5'-precursor tRNA (ptRNA) followed by P RNA-catalyzed processing to release the mature tRNA carrying a homogeneous 5'-monophosphate end
synthesis
-
the bacterial RNase P ribozyme might be used to release RNAs of interest with homogeneous 3'-OH ends from primary transcripts via site-specific cleavage, overview. Also, T7 transcription of mature tRNAs with clustered G residues at the 5'-end may result in 5'-end heterogeneities, which can be avoided by first transcribing the 5'-precursor tRNA (ptRNA) followed by P RNA-catalyzed processing to release the mature tRNA carrying a homogeneous 5'-monophosphate end
synthesis
-
the bacterial RNase P ribozyme might be used to release RNAs of interest with homogeneous 3'-OH ends from primary transcripts via site-specific cleavage, overview. Also, T7 transcription of mature tRNAs with clustered G residues at the 5'-end may result in 5'-end heterogeneities, which can be avoided by first transcribing the 5'-precursor tRNA (ptRNA) followed by P RNA-catalyzed processing to release the mature tRNA carrying a homogeneous 5'-monophosphate end