Biology:RMRP

Generic protein structure example

RNA component of mitochondrial RNA processing endoribonuclease, also known as RMRP, is a human gene.

Mitochondrial RNA-processing endoribonuclease cleaves mitochondrial RNA complementary to the light chain of the displacement loop at a unique site (Chang and Clayton, 1987). The enzyme is a ribonucleoprotein whose RNA component is a nuclear gene product. The RNA component is the first RNA encoded by a single-copy gene in the nucleus and imported into mitochondria. The RMRP gene is untranslated, i.e., it encodes an RNA not a protein.[supplied by OMIM]

It is associated with cartilage–hair hypoplasia.

Further reading

• "A role for RNAase MRP in mitochondrial RNA processing". Cell 70 (1): 16–20. July 1992. doi:10.1016/0092-8674(92)90529-L. PMID 1623519. 
• "A novel endoribonuclease cleaves at a priming site of mouse mitochondrial DNA replication". The EMBO Journal 6 (2): 409–17. February 1987. doi:10.1002/j.1460-2075.1987.tb04770.x. PMID 3582365. 
• "hPop4: a new protein subunit of the human RNase MRP and RNase P ribonucleoprotein complexes". Nucleic Acids Research 27 (12): 2465–72. June 1999. doi:10.1093/nar/27.12.2465. PMID 10352175. 
• "Mutations in the RNA component of RNase MRP cause a pleiotropic human disease, cartilage-hair hypoplasia". Cell 104 (2): 195–203. January 2001. doi:10.1016/S0092-8674(01)00205-7. PMID 11207361. 
• "RMRP gene sequence analysis confirms a cartilage-hair hypoplasia variant with only skeletal manifestations and reveals a high density of single-nucleotide polymorphisms". Clinical Genetics 61 (2): 146–51. February 2002. doi:10.1034/j.1399-0004.2002.610210.x. PMID 11940090. 
• "Worldwide mutation spectrum in cartilage-hair hypoplasia: ancient founder origin of the major70A-->G mutation of the untranslated RMRP". European Journal of Human Genetics 10 (7): 439–47. July 2002. doi:10.1038/sj.ejhg.5200824. PMID 12107819. 
• "Mutual interactions between subunits of the human RNase MRP ribonucleoprotein complex". Nucleic Acids Research 32 (7): 2138–46. 2004. doi:10.1093/nar/gkh539. PMID 15096576. 
• "Evolutionary comparison provides evidence for pathogenicity of RMRP mutations". PLOS Genetics 1 (4): e47. October 2005. doi:10.1371/journal.pgen.0010047. PMID 16244706. 
• "Severely incapacitating mutations in patients with extreme short stature identify RNA-processing endoribonuclease RMRP as an essential cell growth regulator". American Journal of Human Genetics 77 (5): 795–806. November 2005. doi:10.1086/497708. PMID 16252239. 
• "Consequences of mutations in the non-coding RMRP RNA in cartilage-hair hypoplasia". Human Molecular Genetics 14 (23): 3723–40. December 2005. doi:10.1093/hmg/ddi403. PMID 16254002. 
• "Identification of novel RMRP mutations and specific founder haplotypes in Japanese patients with cartilage-hair hypoplasia". Journal of Human Genetics 51 (8): 706–10. 2006. doi:10.1007/s10038-006-0015-3. PMID 16832578. 
• "RMRP mutations in cartilage-hair hypoplasia". American Journal of Medical Genetics. Part A 140 (19): 2121–30. October 2006. doi:10.1002/ajmg.a.31331. PMID 16838329. 
• "RMRP mutations in hematological disorders". Clinical Genetics 71 (5): 468–70. May 2007. doi:10.1111/j.1399-0004.2007.00776.x. PMID 17489853. https://zenodo.org/record/1230629. 
• "Type and level of RMRP functional impairment predicts phenotype in the cartilage hair hypoplasia-anauxetic dysplasia spectrum". American Journal of Human Genetics 81 (3): 519–29. September 2007. doi:10.1086/521034. PMID 17701897. 

External links

• RMRP,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
• GeneReviews/NCBI/NIH/UW entry on Cartilage-Hair Hypoplasia - Anauxetic Dysplasia Spectrum Disorders