| 词条 | Nuclear RNase P |
| 释义 |
| Name = Nuclear RNase P | image = RF00009.jpg | width = | caption = Predicted secondary structure and sequence conservation of RNaseP_nuc | Symbol = RNaseP_nuc | AltSymbols = | Rfam = RF00009 | miRBase = | miRBase_family = | RNA_type = Gene; ribozyme | Tax_domain = Eukaryota; Bacteria; Archaea | GO = {{GO|0008033}} {{GO|0004526}} {{GO|0030677}} | SO = {{SO|0000386}} | CAS_number = | EntrezGene = | HGNCid = | OMIM = | PDB = | RefSeq = | Chromosome = | Arm = | Band = | LocusSupplementaryData = }} In molecular biology, nuclear ribonuclease P (RNase P) is a ubiquitous endoribonuclease, found in archaea, bacteria and eukarya as well as chloroplasts and mitochondria. Its best characterised enzyme activity is the generation of mature 5'-ends of tRNAs by cleaving the 5'-leader elements of precursor-tRNAs. Cellular RNase Ps are ribonucleoproteins. The RNA from bacterial RNase P retains its catalytic activity in the absence of the protein subunit, i.e. it is a ribozyme. Similarly, archaeal RNase P RNA has been shown to be weakly catalytically active in the absence of its respective protein cofactors.[1] Isolated eukaryotic RNase P RNA has not been shown to retain its catalytic function, but is still essential for the catalytic activity of the holoenzyme. Although the archaeal and eukaryotic holoenzymes have a much greater protein content than the bacterial ones, the RNA cores from all three lineages are homologous—the helices corresponding to P1, P2, P3, P4, and P10/11 are common to all cellular RNase P RNAs. Yet there is considerable sequence variation, particularly among the eukaryotic RNAs. References1. ^Tsai, HY; Pulukkunat, DK; Woznick, WK; Gopalan V (2006). "Functional reconstitution and characterization of Pyrococcus furiosus RNase P". PNAS 103: 16147-16152. Further reading
External links
1 : Non-coding RNA |
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