Multiple structural flavors of RNase P in precursor tRNA processing

Wiley Interdisciplinary Reviews - RNA, Journal Year: 2024, Volume and Issue: 15(2)

Published: March 1, 2024

The precursor transfer RNAs (pre-tRNAs) require extensive processing to generate mature tRNAs possessing proper fold, structural stability, and functionality required sustain cellular viability. road tRNA maturation follows an ordered process: 5'-processing, 3'-processing, modifications at specific sites, if any, 3'-CCA addition before aminoacylation recruitment the protein synthesis machinery. Ribonuclease P (RNase P) is a universally conserved endonuclease in all domains of life, performing hydrolysis pre-tRNA sequences 5' end by removal phosphodiester linkages between nucleotides position -1 +1. Except for archaeal species: Nanoarchaeum equitans where are transcribed from leaderless-position +1, RNase indispensable life displays fundamental variations terms enzyme subunit composition, mechanism substrate recognition active site architecture, utilizing cases two metal ion-mediated catalytic reaction. While canonical RNA-based ribonucleoprotein has been well-known occur bacteria, archaea, eukaryotes, occurrence RNA-free protein-only eukaryotes homologs Aquifex prokaryotes discovered more recently. This review aims provide comprehensive overview diversity displayed various holoenzymes towards harnessing critical RNA-protein protein-protein interactions achieving functionality. Furthermore, alternate roles functional interchangeability discussed context its employability several clinical biotechnological applications. article categorized under: RNA Processing > Evolution Genomics Ribonucleoprotein Interactions with Proteins Other Molecules RNA-Protein Complexes.

Language: Английский

Identification of Two Elusive Human Ribonuclease MRP-Specific Protein Components

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2025, Volume and Issue: unknown

Published: Jan. 22, 2025

All known protein components of one the longest-studied human ribonucleoprotein ribozyme nuclear Ribonuclease MRP (RNase MRP), which processes pre-rRNA at ITS1 site 2, are shared with P P), cleaves pre-tRNA 5' leader sequences. Our genome-wide forward genetic screening identified two poorly characterized genes, we named RPP24 and RPP64. We show that these genes required for 2 processing their products efficiently associate RNA MRP. Unlike all other RNase components, RPP64 not activity do P-specific H1. Despite extremely limited sequence homology, exhibit predicted structural similarities to MRP-specific in S. cerevisiae , specific differences regions substrate recognition. Collectively, our functional validation revealed first unique

Language: Английский