Nuclear RNase P
| Nuclear RNase P | |
|---|---|
| SO | SO:0000386 |
| PDB structures | PDBe |
In
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
- PMID 17053064.
Further reading
- Frank DN, Pace NR (1998). "Ribonuclease P: unity and diversity in a tRNA processing ribozyme". Annual Review of Biochemistry. 67: 153–180. PMID 9759486.
- Brown JW (January 1999). "The Ribonuclease P Database". Nucleic Acids Research. 27 (1): 314. PMID 9847214.
- Frank DN, Adamidi C, Ehringer MA, Pitulle C, Pace NR (December 2000). "Phylogenetic-comparative analysis of the eukaryal ribonuclease P RNA". RNA. 6 (12): 1895–1904. PMID 11142387.
- Xiao S, Scott F, Fierke CA, Engelke DR (2002). "Eukaryotic ribonuclease P: a plurality of ribonucleoprotein enzymes". Annual Review of Biochemistry. 71: 165–189. PMID 12045094.
- Marquez SM, Harris JK, Kelley ST, Brown JW, Dawson SC, Roberts EC, Pace NR (May 2005). "Structural implications of novel diversity in eucaryal RNase P RNA". RNA. 11 (5): 739–751. PMID 15811915.