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Literature summary for 3.1.26.5 extracted from
- Inhibition of gene expression by RNase P (2010), New Biotechnol., 27, 212-221.
Application
| Application | Comment | Organism |
|---|---|---|
| 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 | Escherichia coli |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| plasmids carrying the M1GS constructs delivered to murine cytomegalovirus-infected mice by a hydrodynamic transfection procedure | Escherichia coli |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| chloroplast | - |
Spinacia oleracea | 9507 | - |
| mitochondrion | - |
Homo sapiens | 5739 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
| Homo sapiens | - |
- |
- |
| Ignicoccus hospitalis | - |
- |
- |
| no activity in Nanoarchaeum equitans | - |
- |
- |
| Spinacia oleracea | - |
- |
- |
| Synechocystis sp. | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | Homo sapiens | ? | - |
? |  |
| additional information | cleaves the internal ribosome entry site region in hepatitis C virus RNA near the AUG start codon | Synechocystis sp. | ? | - |
? | |
| 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 | Escherichia coli | ? | - |
? | |
| 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 | Spinacia oleracea | ? | - |
? | |
| 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 | Escherichia coli | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| C5 protein | - |
Escherichia coli |
| M1 RNA | - |
Escherichia coli |
| ribonuclease P | - |
Escherichia coli |
| ribonuclease P | - |
Homo sapiens |
| ribonuclease P | - |
Spinacia oleracea |
| ribonuclease P | - |
Synechocystis sp. |
| ribonuclease P | - |
Ignicoccus hospitalis |
| RNase P | - |
Escherichia coli |
| RNase P | - |
Homo sapiens |
| RNase P | - |
Spinacia oleracea |
| RNase P | - |
Synechocystis sp. |
| RNase P | - |
Ignicoccus hospitalis |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Homo sapiens | RNase P-external guide sequence and short hairpin RNAi technologies have about equal levels of inhibition of RNase P protein subunits | down |
| Escherichia coli | when plasmids carrying the M1GS constructs are delivered to murine cytomegalovirus-infected mice by a hydrodynamic transfection procedure, the M1GS RNA is expressed in a substantial amount in the livers and spleens of the animals | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 | Ignicoccus hospitalis |
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