Bacterial RNase P class A

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Bacterial RNase P class A

Type:	Gene; ribozyme;
2° structure:	Published; PubMed
Seed alignment:	Brown JW, The Ribonuclease P Database, PubMed
Avg length:	310.0 nucleotides
Avg identity:	59%

It has been suggested that this article or section be merged with RNase P. (Discuss)

Ribonuclease P (RNase P) is a ubiquitous endoribonuclease, found in archaea, bacteria and eukarya as well as chloroplasts and mitochondria. Its best characterised activity is the generation of mature 5'-ends of tRNAs by cleaving the 5'-leader elements of precursor-tRNAs. Cellular RNase Ps are ribonucleoproteins. RNA from bacterial RNase Ps retains its catalytic activity in the absence of the protein subunit, i.e. it is a ribozyme. Isolated eukaryotic and archaeal 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 holoenzyme s have a much greater protein content than the bacterial ones, the RNA cores from all the three lineages are homologous -- 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.

[edit] References

[1] Frank, DN; Pace NR (1998). "Ribonuclease P: unity and diversity in a tRNA processing ribozyme". Annu Rev Biochem 67: 153–180. doi:10.1146/annurev.biochem.67.1.153. PMID 9759486.
[2] Brown, JW (1999). "The Ribonuclease P Database". Nucleic Acids Res 27: 314–. doi:10.1093/nar/27.1.314. PMID 9847214.