RNase MRP
RNase MRP is an enzymatically active ribonucleoprotein with two distinct roles in eukaryotes. RNAse MRP stands for RNAse for mitochondrial RNA processing. In mitochondria it plays a direct role in the initiation of mitochondrial DNA replication. In the nucleus it is involved in precursor rRNA processing, where it cleaves the internal transcribed spacer 1 between 18S and 5.8S rRNAs. Despite distinct functions, RNase MRP has been shown to be evolutionarily related to RNase P. Like eukaryotic RNase P, RNase MRP is not catalytically active without associated protein subunits.
Mutations in the RNA component of RNase MRP cause cartilage–hair hypoplasia, a pleiotropic human disease. Responsible for this disease is a mutation in the RNase MRP RNA gene, a non-coding RNA gene. RMRP was the first non-coding nuclear RNA gene found to cause disease.
Mechanism and mutation effects
RNAase MRP and its role in pre-rRNA processing has been previously studied in Yeast cells. RNase MRP has been shown to cleave an internal transcribed spacer, specifically ITS1 at the specific site A3 of the rRNA precursor, leading, after additional trimming, to the formation of the mature 5′-end of 5.8S rRNA.Recent data that has been gathered using several temperature-sensitive RNase MRP mutants that showed that inactivation of RNase MRP leading to severe reduction of the abundance of all early intermediates in the typical rRNA processing pathway. However, the transcription of the rRNA precursor is not affected, thus suggesting that RNase MRP plays a key role in the processing of rRNA beyond the cleavage of the A3 site in ITS1.
Further research in Yeast cell RNase MRP has shown a potential role in the regulation of the cell cycle. RNase MRP mutations led to missegregation of plasmids and caused cell cycle delay at the end of mitosis, followed by a buildup of cyclin B2 protein. RNase MRP also demonstrated cleavage ability of the 5′-UTR of CLB2 mRNA that allows for rapid 5′-to-3′ degradation by XRN1, an exoribonuclease enzyme.
Link to RNAse P
and RNAse MRP are ribonucleoprotein complexes that are important in RNA processing. Both subunits have a highly conserved P4 helical region, which is a type of nucleic acid tertiary structure. This region is needed for catalytic function, and is probably an important part of the enzyme's active site. RNAse P is found in both eukaryotes and prokaryotes and it cleaves a pre-tRNA to generate the mature 5’ end of the tRNA. RNase MRP is found only in eukaryotes, and is involved in rRNA processing, which is the conversion of preribosomal RNA into mature rRNA through splicing, modifications, and cleavage. The exact mechanism is described above.Evolutionary link
These two ribonucleases are most likely evolutionarily related through a common ancestor, since they have common protein subunits and can be folded into very similar secondary structures. There are many conserved regions in these two ribonucleases. Sequences of the CR-I, CR-V, and CR-IV genes in domain 1 of the P4 helical region are conserved, with the consensus sequence in CR-IV being AGNNNNA for RNAse P and AGNNA for RNase MRP. CR-II and CR-III are also conserved in domain 2 of P RNA. The P3 helix is also conserved in both ribonucleases in all eukaryotes, but the function of this helix is not yet clear. These conserved regions are evidence of the close phylogenetic relation between these two important ribonucleoprotein complexes.Diseases associated with RNAse MRP gene
without hypotrichosis, anauxetic dysplasia, kyphomelic dysplasia, Omenn syndrome are diseases associated with mutated and dysfunctional RNAse MRP activity, hence, the RMRP gene.Disease | Abbreviation | Location of mutation | Mutation in RNAse MRP protein or RNA in RNAse MRP? | Symptoms |
Cartilage–hair hypoplasia | CHH | 1.Insertion, duplication or triplication at promoter or 2. In RNA transcribed by RNAse MRP | RNA in RNAse MRP | Patients have short stature, skeletal anomalies, blood and immune problems, and fine, light-colored hair |
Metaphyseal dysplasia without hypotrichosis | MDWH | 1. on RMRP Gene-->common insertion being -21-20insTCTGTGAAGCTGGGGAC on paternal allele or 2. 218A-->G point mutation occurring on maternal allele | RNA in RNAse MRP | Patients unable to produce new tubular structures in metaphyses of long bones. This results in porous and expanded long bones |
Anauxetic dysplasia | AD | Homozygous insertion mutation and two compound heterozygous mutations | RNA in RNAse MRP | Early onset of extremely short stature. Adults typically not exceeding 85 cm in height. Abnormal amount of teeth. Slight mental retardation. |
Kyphomelic dysplasia | KD | Mutation of T at 194-195 paternal allele and a 63 C-->T point mutation of the maternal allele. | Undetermined | Form of short-limbed dwarfism. Bowing long bones, dysmorphia, flattened vertebrae, and short ribs. |
Omenn Syndrome | OS | Three mutations in RMRP gene | RNA in RNAse MRP | Patients are immunodeficient and have scaly erythroderma and severe reddening of skin. |
Cartilage–hair hypoplasia
in the RNA component of RNase MRP cause cartilage–hair hypoplasia, a pleiotropic human disease. Two categories of mutations involving RNAse MRP have been identified in patients with CHH. The first type is when an insertion, duplication, or triplication occurs at the promoter of the RNAse MRP gene between the TATA box and the transcription initiation site. This causes the initiation of RNAse MRP to be slow, or to not occur at all.The second category consists of mutations that are in the transcribed RNA made by the RNAse MRP. Patients with CHH have been identified to have over 70 different mutations in the RNA transcript made by RNAse MRP, whereas around 30 distinct mutations have been identified in the promoter region of the RNAse MRP gene. Most CHH patients have a combination of either a promoter mutation in one allele along with a RNAse MRP RNA mutation in the other allele, or a combination of two RNAse MRP RNA mutations in both alleles. The fact that there is not often a mutation in the promoter region in both alleles shows the lethality of not having this RNA present that is transcribed by RNAse MRP.