RNase P processing 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]Cite error: Closing </ref> missing for <ref> tag In yeast, the proteins of RNase P also bind telomerase.[3]
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.
A topic page on the RNP-based S. cerevisiae RNase P is found here
↑Gobert A, Pinker F, Fuchsbauer O, Gutmann B, Boutin R, Roblin P, Sauter C, Giege P. Structural insights into protein-only RNase P complexed with tRNA. Nat Commun. 2013;4:1353. doi: 10.1038/ncomms2358. PMID:23322041 doi:https://dx.doi.org/10.1038/ncomms2358
↑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
transfer RNAs - RNP-based RNase P - S. cerevisiae here - RNP-based RNase P bound to pre-tRNA substrate- S. cerevisiae
Protein-based
Structural insights into protein-only RNase P complexed with tRNA
