RNase P is a ribonuclease that processes the 5′ end of pre-transfer RNAs as well as other RNA molecules.[1]. Most RNase Ps are complexes of proteins and RNAs, termed ribonucleoprotein (RNP) complexes; however, a few protein-only RNase Ps have been described.[2][3]
In eukaryotes, the RNase P proteins have been found to have other roles. For example, many of the proteins are shared with a related RNase P, the small nucleolar RNase MRP, that is involved in processing ribosomal RNA.[4] In yeast, the proteins of RNase P also bind telomerase.[5]
Sydney Altman shared in the 1989 Nobel Prize for his work on the catalytic properties of the RNP-based RNase P, as described here.
Structural insights
The active site of RNase P contains metal ions. Specifically, in the RNP-based RNase P, the ions at the active site are magnesium, and they seem to be zinc-based metallonucleases in the case of Arabidopsis proteinaceous RNase P.
Articles in Proteopedia concerning RNase P include:
A topic page on the RNP-based S. cerevisiae RNase P is found here
↑Davila Lopez M, Rosenblad MA, Samuelsson T. Conserved and variable domains of RNase MRP RNA. RNA Biol. 2009 Jul;6(3):208-20. Epub 2009 Jul 30. PMID:19395864
↑Lemieux B, Laterreur N, Perederina A, Noel JF, Dubois ML, Krasilnikov AS, Wellinger RJ. Active Yeast Telomerase Shares Subunits with Ribonucleoproteins RNase P and RNase MRP. Cell. 2016 May 19;165(5):1171-1181. doi: 10.1016/j.cell.2016.04.018. Epub 2016, May 5. PMID:27156450 doi:https://dx.doi.org/10.1016/j.cell.2016.04.018
3D Structures of RNase P
Updated on 02-September-2019
Cryo-electron microscopy structure of an archaeal ribonuclease P holoenzyme.
RNP-based RNase P
ribonuclease - RNP-based RNase P - S. cerevisiae transfer RNAs - RNP-based RNase P bound to pre-tRNA substrate - S. cerevisiae
Protein-only RNase P
here - nuclear PRORP2 - Arabidopsis thaliana here -mitochondrial and chloroplast PRORP1 - Arabidopsis thaliana
