RNase MRP and disease

Advanced Review

Sandy Mattijssen, Tim J. M. Welting, Ger J. M. Pruijn

Published Online: May 06 2010

DOI: 10.1002/wrna.9

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Abstract The human RNase MRP complex consists of a catalytic RNA and several protein components. RNase MRP is a ubiquitously expressed eukaryotic endoribonuclease that cleaves various RNAs, including ribosomal, messenger, and mitochondrial RNAs, in a highly specific fashion. In several autoimmune diseases autoantibodies targeting RNase MRP have been found. These so‐called anti‐Th/To autoantibodies, which most frequently can be detected in the sera of scleroderma patients, are directed to several protein components of the RNase MRP and the evolutionarily related RNase P complex. It is not yet known whether the anti‐Th/To immune response is an epiphenomenon or whether these autoantibodies play a role in the pathophysiology of the disease. The gene encoding the RNase MRP RNA was the first nuclear non‐coding RNA gene demonstrated to be associated with a genetic disease. Mutations in this gene are causing the highly pleiotropic disease cartilage‐hair hypoplasia (CHH). CHH patients are characterized by a short stature, hypoplastic hair, and short limbs. In addition, they show a predisposition to lymphomas and other cancers and suffer from defective T‐cell immunity. Since the identification of the first CHH‐associated mutations in 2001, many distinct mutations have been found in different patients. These mutations either affect the structure of the RNase MRP RNA or are located in the promoter region and reduce the expression levels. In this review article we will, after describing the biochemical aspects of RNase MRP, discuss the targeting of RNase MRP in autoimmunity and the role of mutations in the RNase MRP RNA gene in CHH. Copyright © 2010 John Wiley & Sons, Ltd. This article is categorized under: RNA-Based Catalysis > RNA‐Mediated Cleavage Translation > Ribosome Biogenesis RNA Turnover and Surveillance > Regulation of RNA Stability RNA in Disease and Development > RNA in Disease

Structural models of the human RNase MRP and RNase P complexes. (a): RNase MRP. (b): RNase P. The RNA components are in black, proteins are depicted in gray shades. Structural elements of the RNA components are designated P1–P19 and J3/4 in accordance with previous definitions.

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RMRP mutations associated with CHH that affect the structure of the RMRP RNA. CHH‐associated mutations are marked by the arrows (single nucleotide substitutions and insertions) and boxes (duplications and deletions) combined with the identity of the mutation; polymorphisms are indicated by circled residues. Conservation of nucleotides has been determined by Thiel and collaborators85 based upon the RMRP RNA sequences from nine species (human (Homo sapiens), mouse (Mus musculus), rat (Rattus norvegicus), rabbit (Oryctolagus cuniculus), dog (Canis familiaris), armadillo (Dasypus novemcinctus), elephant (Loxodonta africana), opossum (Monodelphis domestica), and pipid frog (Xenopus tropicalis). Black nucleotides in the RMRP RNA sequence are 100% conserved among these species; dark gray nucleotides mark conservation in eight species; light gray nucleotides are conserved in six to seven species; outlined nucleotides are conserved in less than six species.

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The involvement of RNase MRP in biochemical processes. The identified functional activities of RNase MRP are schematically illustrated. These also indicate that the impairment of RMRP activity, for example by RMRP mutations, contributes to the etiology of human disease by various mechanisms. The human RNase MRP complex is depicted as a cartoon of the RMRP RNA molecule and the interacting proteins Rpp20, Rpp25, Rpp30, Rpp38, Rpp40, hPop5, and hPop1. See the text for a more detailed description of the role of RNase MRP in these processes.

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