Nuclear RNase P

Nuclear RNase P
Predicted secondary structure and sequence conservation of RNaseP_nuc
Identifiers
Symbol RNaseP_nuc
Rfam RF00009
Other data
RNA type Gene; ribozyme
Domain(s) Eukaryota; Bacteria; Archaea
GO 0008033 0004526 0030677
SO 0000386

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.

References

  1. ↑ 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

This article is issued from Wikipedia - version of the 7/19/2014. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.