EC Number   |
Application |
Reference |
|---|
   3.1.26.5 | 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) |
708512 |
| 3.1.26.5 | 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 |
710549 |
| 3.1.26.5 | 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 |
134453 |
| 3.1.26.5 | 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 |
715925 |
| 3.1.26.5 | 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 |
730325 |
| 3.1.26.5 | 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 |
709542 |
| 3.1.26.5 | 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 |
-, 750647 |
| 3.1.26.5 | medicine |
catalytic RNase P RNA from Synechocystis sp. may be an active agent for Hepatitis C virus interventions |
664949 |
| 3.1.26.5 | 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 |
752195 |
| 3.1.26.5 | medicine |
feasibility to develop Salmonella-mediated gene transfer of RNase P ribozymes as an effective approach for gene-targeting applications |
710437 |
