The Bacillus subtilis RNase P holoenzyme contains two RNase P RNA and two RNase P protein subunits

Archaeal RNase P has multiple protein subunits homologous to eukaryotic nuclear RNase P proteins.

Although archaeal RNase P RNAs are similar in both sequence and structure to those of Bacteria rather than eukaryotes, and heterologous reconstitution between the Bacillus subtilis RNase P protein and some archaeal RNase P RNAs has been demonstrated, no archaeal protein sequences with similarity to any known bacterial RNase P protein subunit have been identified, and the density of Methanotherm...

RNase P RNA-mediated catalysis.

The endoribonuclease RNase P is involved in the processing of tRNA precursors to generate mature 5' termini. The catalytic activity of RNase P is associated with an RNA, RNase P RNA. A specific interaction between the 3' end of the substrate and RNase P RNA, to form an RNase P RNA-substrate complex, is referred to as the '73-294-interaction'. This interaction has an important role for efficient...

Difference between mitochondrial RNase P and nuclear RNase P.

Ion dependence of the Bacillus subtilis RNase P reaction.

The properties of the Bacillus subtilis RNase P are characterized with regard to the types and concentrations of monovalent and divalent ions required to potentiate precursor tRNA cleavage by the protein-RNA holoenzyme and the catalytic RNA alone. The ionic dependence of the RNase P RNA-catalyzed reaction in part seems due to a requirement for ion shielding between substrate and catalytic RNAs....

Archaeal/Eukaryal RNase P: subunits, functions and RNA diversification

RNase P, a catalytic ribonucleoprotein (RNP), is best known for its role in precursor tRNA processing. Recent discoveries have revealed that eukaryal RNase P is also required for transcription and processing of select non-coding RNAs, thus enmeshing RNase P in an intricate network of machineries required for gene expression. Moreover, the RNase P RNA seems to have been subject to gene duplicati...