Abstract
RNase MRP RNA is the RNA subunit of the RNase mitochondrial RNA processing (MRP) enzyme complex that is involved in multiple cellular RNA processing events. Mutations on RNase MRP RNA gene (RMRP) cause a recessively inherited developmental disorder, cartilage-hair hypoplasia (CHH). The relationship of the genotype (RMRP mutation), RNA processing deficiency of the RNase MRP complex, and the phenotype of CHH and other skeletal dysplasias is yet to be explored.
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References
McKusick VA . Mendelian inheritance in man. A catalog of human genes and genetic disorders. Baltimore: Johns Hopkins University Press, 1998; Online Mendelian Inheritance in Man (OMIM) is hosted at http://www.ncbi.nlm.nih.gov/omim/.
Chang DD, Clayton DA . Mouse RNAase MRP RNA is encoded by a nuclear gene and contains a decamer sequence complementary to a conserved region of mitochondrial RNA substrate. Cell 1989; 56:131–139.
Lygerou Z, Allmang C, Tollervey D, Seraphin B . Accurate processing of a eukaryotic precursor ribosomal RNA by ribonuclease MRP in vitro. Science 1996; 272:268–270.
Schmitt ME, Clayton DA . Nuclear RNase MRP is required for correct processing of pre-5.8S rRNA in Saccharomyces cerevisiae. Mol Cell Biol 1993; 13:7935–7941.
Li K, Smagula CS, Parsons WJ, et al. Subcellular partitioning of MRP RNA assessed by ultrastructural and biochemical analysis. J Cell Biol 1994; 124:871–882.
van Eenennaam H, Jarrous N, van Venrooij WJ, Pruijn GJ . Architecture and function of the human endonucleases RNase P and RNase MRP. IUBMB Life 2000; 49:265–272.
Chamberlain JR, Lee Y, Lane WS, Engelke DR . Purification and characterization of the nuclear RNase P holoenzyme complex reveals extensive subunit overlap with RNase MRP. Genes Dev 1998; 12:1678–1690.
Gill T, Aulds J, Schmitt ME . A specialized processing body that is temporally and asymmetrically regulated during the cell cycle in Saccharomyces cerevisiae. J Cell Biol 2006; 173:35–45.
Gill T, Cai T, Aulds J, Wierzbicki S, Schmitt ME . RNase MRP cleaves the CLB2 mRNA to promote cell cycle progression: novel method of mRNA degradation. Mol Cell Biol 2004; 24:945–953.
McKusick VA, Eldridge R, Hostetler JA, Ruangwit U, Egeland JA . Dwarfism in the Amish. Ii. Cartilage-hair hypoplasia. Bull Johns Hopkins Hosp 1965; 116:285–326.
Ridanpää M, Sistonen P, Rockas S, et al. Worldwide mutation spectrum in cartilage-hair hypoplasia: ancient founder origin of the major70A→G mutation of the untranslated RMRP. Eur J Hum Genet 2002; 10:439–447.
Ridanpää M, van Eenennaam H, Pelin K, et al. Mutations in the RNA component of RNase MRP cause a pleiotropic human disease, cartilage-hair hypoplasia. Cell 2001; 104:195–203.
Bonafé L, Schmitt K, Eich G, Giedion A, Superti-Furga A . RMRP gene sequence analysis confirms a cartilage-hair hypoplasia variant with only skeletal manifestations and reveals a high density of single-nucleotide polymorphisms. Clin Genet 2002; 61:146–151.
Hirose Y, Nakashima E, Ohashi H, et al. Identification of novel RMRP mutations and specific founder haplotypes in Japanese patients with cartilage-hair hypoplasia. J Hum Genet 2006; 51:706–710.
Hermanns P, Tran A, Munivez E, et al. RMRP mutations in cartilage-hair hypoplasia. Am J Med Genet A 2006 140:2121–2130.
Nakashima E, Mabuchi A, Kashimada K, et al. RMRP mutations in Japanese patients with cartilage-hair hypoplasia. Am J Med Genet A 2003; 123:253–256.
Ridanpää M, Jain P, McKusick VA, Francomano CA, Kaitila I . The major mutation in the RMRP gene causing CHH among the Amish is the same as that found in most Finnish cases. Am J Med Genet C Semin Med Genet 2003; 121:81–83.
Hermanns P, Bertuch AA, Bertin TK, et al. Consequences of mutations in the non-coding RMRP RNA in cartilage-hair hypoplasia. Hum Mol Genet 2005; 14:3723–3740.
Bonafé L, Dermitzakis ET, Unger S, et al. Evolutionary comparison provides evidence for pathogenicity of RMRP mutations. PLoS Genet 2005; 1:e47.
Thiel CT, Horn D, Zabel B, et al. Severely incapacitating mutations in patients with extreme short stature identify RNA-processing endoribonuclease RMRP as an essential cell growth regulator. Am J Hum Genet 2005; 77:795–806.
Roifman CM, Gu Y, Cohen A . Mutations in the RNA component of RNase mitochondrial RNA processing might cause Omenn syndrome. J Allergy Clin Immunol 2006; 117:897–903.
Kuijpers TW, Ridanpää M, Peters M, et al. Short-limbed dwarfism with bowing, combined immune deficiency, and late onset aplastic anaemia caused by novel mutations in the RMPR gene. J Med Genet 2003; 40:761–766.
Prasad C, Cramer BC, Pushpanathan C, Crowley MC, Ives EJ . Kyphomelic dysplasia: a rare form of semilethal skeletal dysplasia. Clin Genet 2000; 58:390–395.
Bommer U-A, Stahl J, Henske A, Lutsch G, Bielka H . Identification of proteins of the 40S ribosomal subunit involved in interaction with initiation factor eIF-2 in the quaternary initiation complex by means of monospecific antibodies. FEBS Lett 1988; 233:114–118.
Abou Elela S, Nazar RN . Role of the 5.8S rRNA in ribosome translocation. Nucleic Acids Res 1997; 25:1788–1794.
Samanta MP, Tongprasit W, Sethi H, Chin CS, Stolc V . Global identification of noncoding RNAs in Saccharomyces cerevisiae by modulating an essential RNA processing pathway. Proc Natl Acad Sci USA 2006; 103:4192–4197.
Altman S, Kirsebom L . Ribonuclease P . In: Gesteland R, Cech T, Atkins J, eds. The RNA world. New York: Cold Spring Harbor Laboratory Press, 1999:351–380.
Ridanpää M, Ward LM, Rockas S, et al. Genetic changes in the RNA components of RNase MRP and RNase P in Schmid metaphyseal chondrodysplasia. J Med Genet 2003; 40:741–746.
Shadel GS, Clayton DA . Mitochondrial DNA maintenance in vertebrates. Annu Rev Biochem 1997; 66:409–435.
Venema J, Tollervey D . Ribosome synthesis in Saccharomyces cerevisiae. Annu Rev Genet 1999; 33:261–311.
Cai T, Aulds J, Gill T, Cerio M, Schmitt ME . The Saccharomyces cerevisiae RNase mitochondrial RNA processing is critical for cell cycle progression at the end of mitosis. Genetics 2002; 161:1029–1042.
Acknowledgements
Research on RNase MRP in Li Y's laboratory is supported by a pilot study grant for Systems Biology from the Center for Genetics and Molecular Medicine, University of Louisville. Li Y is supported by a Beginning-Grant-In-Aid grant from the American Heart Association. Li Y is grateful to fantastic colleagues Drs Mark D Brennan, Marlene C Steffen, and Yanglong Zhu for critical reading of the manuscript.
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Martin, A., Li, Y. RNase MRP RNA and human genetic diseases. Cell Res 17, 219–226 (2007). https://doi.org/10.1038/sj.cr.7310120
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DOI: https://doi.org/10.1038/sj.cr.7310120
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