Function'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 complexes; however, a few protein-only RNase Ps have been described.[2] 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.[3] In yeast, the proteins of RNase P also bind telomerase.[4] Structural insightsThe active site of RNase P contains metal ions. Specifically, in the RNA-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.
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Updated on 02-September-2019
Cryo-electron microscopy structure of an archaeal ribonuclease P holoenzyme.
Structural insights into protein-only RNase P complexed with tRNA
transfer RNAs - RNP-based RNase P - S. cerevisiae
6ah3 - RNP-based RNase P bound to pre-tRNA - S. cerevisiae
1jox
1jp0
1u9s
2a2e 2k3r 2ki7 2vrt
3iab 3q1q 3q1r
4g23 4g24 4g25 4g26 4xgl
4xgm
5diz 5xtm
6ahv 6bv5 6bv6 6bv8 6bv9
This page was last modified 18:49, 2 September 2019.