MRP

ALTERNATE NAMES: NME1, RRP2

LENGTH: 340 nts

PROCESS: Cleavage of rRNA, processing of RNA primers involved in mitochondrial DNA replication, cleavage of CLB2 mRNA in its 5'UTR.

TARGET SITE(S):
Not reported

GENOMIC ORGANIZATION: Independent gene
 

SGD ORF MAP
ORFmap

GENE DISRUPTION PHENOTYPE: Lethal

ORTHOLOGS IN HUMANS AND OTHER EUKARYOTES:
Click here and see that yeast and humans have orthologous snoRNAs.
 
Click here and see that other Eukaryotes have orthologous snoRNAs.

PHYLOGENETIC CONSERVATION IN FUNGI:
Click here to examine conservation of this snoRNA in fungal genomes using BLAST.

RNA SEQUENCE:

   1 aauccaugac caaagaaucg ucacaaaucg aagcuuacaa aauggaguaa aauuuuuuuu
  61 acucaguaau augcuuuggg uugaaagucu cccaccaauu cguaugcgga aaacguaaug
 121 agauuuaaaa auuuuaaauu guuuaaauca acucauuaag gaggaugccc uuggguauuc
 181 ugcuucuuga ccugguaccu cuauugcagg guacuggugu uuucuucggu acuggauucc
 241 guuuguaugg aaucuaaacc auaguuauga cgauugcucu uucccgugcu ggaucgagua
 301 acccaaugga gcuuacuauu cuugguccau ggauucaccc
 

YEAST GENOME DATABASE ENTRY:
Click here to view the SGD entry for this snoRNA.

REFERENCES:
Forster, A. C., and S. Altman. 1990. Similar cage-shaped structures for the RNA components of all ribonuclease P and ribonuclease MRP enzymes. Cell 62:407-409.
Shuai, K., and J. R. Warner. 1991. A temperature sensitive mutant of Saccharomyces cerevisiae defective in pre-rRNA processing. Nucleic Acids Res 19:5059-5064.
Schmitt, M. E., and D. A. Clayton. 1992. Yeast site-specific ribonucleoprotein endoribonuclease MRP contains an RNA component homologous to mammalian RNase MRP RNA and essential for cell viability. Genes Dev 6:1975-1985.
Topper, J. N., J. L. Bennett, and D. A. Clayton. 1992. A role for RNAase MRP in mitochondrial RNA processing. Cell 70:16-20.
Stohl, L. L., and D. A. Clayton. 1992. Saccharomyces cerevisiae contains an RNase MRP that cleaves at a conserved mitochondrial RNA sequence implicated in replication priming. Mol Cell Biol 12:2561-2569.
Kiss, T., C. Marshallsay, and W. Filipowicz. 1992. 7-2/MRP RNAs in plant and mammalian cells: association with higher order structures in the nucleolus. Embo J 11:3737-3746.
Lindahl, L., R. H. Archer, and J. M. Zengel. 1992. A new rRNA processing mutant of Saccharomyces cerevisiae. Nucleic Acids Res 20:295-301.
Schmitt, M. E., and D. A. Clayton. 1993. Nuclear RNase MRP is required for correct processing of pre-5.8S rRNA in Saccharomyces cerevisiae. Mol Cell Biol 13:7935-7941.
Schmitt, M. E., J. L. Bennett, D. J. Dairaghi, and D. A. Clayton. 1993. Secondary structure of RNase MRP RNA as predicted by phylogenetic comparison. Faseb J 7:208-213.
Chu, S., R. H. Archer, J. M. Zengel, and L. Lindahl. 1994. The RNA of RNase MRP is required for normal processing of ribosomal RNA. Proc Natl Acad Sci U S A 91:659-663.
Lygerou, Z., P. Mitchell, E. Petfalski, B. Seraphin, and D. Tollervey. 1994. The POP1 gene encodes a protein component common to the RNase MRP and RNase P ribonucleoproteins. Genes Dev 8:1423-1433.
Schmitt, M. E., and D. A. Clayton. 1994. Characterization of a unique protein component of yeast RNase MRP: an RNA-binding protein with a zinc-cluster domain. Genes Dev 8:2617-2628.
Paluh, J. L., and D. A. Clayton. 1995. Schizosaccharomyces pombe RNase MRP RNA is homologous to metazoan RNase MRP RNAs and may provide clues to interrelationships between RNase MRP and RNase P. Yeast 11:1249-1264.
Morrissey, J. P., and D. Tollervey. 1995. Birth of the snoRNPs: the evolution of RNase MRP and the eukaryotic pre-rRNA-processing system. Trends Biochem Sci 20:78-82.
Reilly, T. H., and M. E. Schmitt. 1995. The yeast, Saccharomyces cerevisiae, RNase P/MRP ribonucleoprotein endoribonuclease family. Mol Biol Rep 22:87-93.
Reddy, R., and S. Shimba. 1995. Structural and functional similarities between MRP and RNase P. Mol Biol Rep 22:81-85.
Tollervey, D. 1995. Genetic and biochemical analyses of yeast RNase MRP. Mol Biol Rep 22:75-79.
Lindahl, L., and J. M. Zengel. 1995. RNase MRP and rRNA processing. Mol Biol Rep 22:69-73.
Jacobson, M. R., L. G. Cao, Y. L. Wang, and T. Pederson. 1995. Dynamic localization of RNase MRP RNA in the nucleolus observed by fluorescent RNA cytochemistry in living cells. J Cell Biol 131:1649-1658.
Sbisa, E., G. Pesole, A. Tullo, and C. Saccone. 1996. The evolution of the RNase P- and RNase MRP-associated RNAs: phylogenetic analysis and nucleotide substitution rate. J Mol Evol 43:46-57.
Lygerou, Z., C. Allmang, D. Tollervey, and B. Seraphin. 1996. Accurate processing of a eukaryotic precursor ribosomal RNA by ribonuclease MRP in vitro. Science 272:268-270.
Jeong-Yu, S., A. F. Davis, and D. A. Clayton. 1996. Subtle determinants of the nucleocytoplasmic partitioning of in vivo-transcribed RNase MRP RNA in Xenopus laevis oocytes. Gene Expr 5:155-167.
Allmang, C., Y. Henry, J. P. Morrissey, H. Wood, E. Petfalski, and D. Tollervey. 1996. Processing of the yeast pre-rRNA at sites A(2) and A(3) is linked. Rna 2:63-73.
Lee, B., A. G. Matera, D. C. Ward, and J. Craft. 1996. Association of RNase mitochondrial RNA processing enzyme with ribonuclease P in higher ordered structures in the nucleolus: a possible coordinate role in ribosome biogenesis. Proc Natl Acad Sci U S A 93:11471-11476.
Chu, S., J. M. Zengel, and L. Lindahl. 1997. A novel protein shared by RNase MRP and RNase P. Rna 3:382-391.
Dichtl, B., and D. Tollervey. 1997. Pop3p is essential for the activity of the RNase MRP and RNase P ribonucleoproteins in vivo. Embo J 16:417-429.
Chamberlain, J. R., Y. Lee, W. S. Lane, and D. R. Engelke. 1998. Purification and characterization of the nuclear RNase P holoenzyme complex reveals extensive subunit overlap with RNase MRP. Genes Dev 12:1678-1690.
Schmitt, M. E. 1999. Molecular modeling of the three-dimensional architecture of the RNA component of yeast RNase MRP. J Mol Biol 292:827-836.
Lindahl, L., S. Fretz, N. Epps, and J. M. Zengel. 2000. Functional equivalence of hairpins in the RNA subunits of RNase MRP and RNase P in Saccharomyces cerevisiae. Rna 6:653-658.
Shadel, G. S., G. A. Buckenmeyer, D. A. Clayton, and M. E. Schmitt. 2000. Mutational analysis of the RNA component of Saccharomyces cerevisiae RNase MRP reveals distinct nuclear phenotypes. Gene 245:175-184.
van Eenennaam, H., N. Jarrous, W. J. van Venrooij, and G. J. Pruijn. 2000. Architecture and function of the human endonucleases RNase P and RNase MRP. IUBMB Life 49:265-272.
Klein, D. J., T. M. Schmeing, P. B. Moore, and T. A. Steitz. 2001. The kink-turn: a new RNA secondary structure motif. Embo J 20:4214-4221.
Ridanpaa, M., H. van Eenennaam, K. Pelin, R. Chadwick, C. Johnson, B. Yuan, W. vanVenrooij, G. Pruijn, R. Salmela, S. Rockas, O. Makitie, I. Kaitila, and A. de la Chapelle. 2001. Mutations in the RNA component of RNase MRP cause a pleiotropic human disease, cartilage-hair hypoplasia. Cell 104:195-203.
Cai, T., J. Aulds, T. Gill, M. Cerio, and M. E. Schmitt. 2002. The Saccharomyces cerevisiae RNase mitochondrial RNA processing is critical for cell cycle progression at the end of mitosis. Genetics 161:1029-1042.
Li, X., D. N. Frank, N. Pace, J. M. Zengel, and L. Lindahl. 2002. Phylogenetic analysis of the structure of RNase MRP RNA in yeasts. Rna 8:740-751.
Walker, S. C., and J. M. Avis. 2004. A conserved element in the yeast RNase MRP RNA subunit can participate in a long-range base-pairing interaction. J Mol Biol 341:375-388.
Li, X., S. Zaman, Y. Langdon, J. M. Zengel, and L. Lindahl. 2004. Identification of a functional core in the RNA component of RNase MRP of budding yeasts. Nucleic Acids Res 32:3703-3711.
Gill, T., T. Cai, J. Aulds, S. Wierzbicki, and M. E. Schmitt. 2004. RNase MRP cleaves the CLB2 mRNA to promote cell cycle progression: novel method of mRNA degradation. Mol Cell Biol 24:945-953.
Klein, M., M. Geisler, S. J. Suh, H. U. Kolukisaoglu, L. Azevedo, S. Plaza, M. D. Curtis, A. Richter, B. Weder, B. Schulz, and E. Martinoia. 2004. Disruption of AtMRP4, a guard cell plasma membrane ABCC-type ABC transporter, leads to deregulation of stomatal opening and increased drought susceptibility. Plant J 39:219-236.
Walker, S. C., T. V. Aspinall, J. M. Gordon, and J. M. Avis. 2005. Probing the structure of Saccharomyces cerevisiae RNase MRP. Biochem Soc Trans 33:479-481.
Salinas, K., S. Wierzbicki, L. Zhou, and M. E. Schmitt. 2005. Characterization and purification of Saccharomyces cerevisiae RNase MRP reveals a new unique protein component. J Biol Chem 280:11352-11360.
Dlakic, M. 2005. 3D models of yeast RNase P/MRP proteins Rpp1p and Pop3p. Rna 11:123-127.
Hermanns, P., A. A. Bertuch, T. K. Bertin, B. Dawson, M. E. Schmitt, C. Shaw, B. Zabel, and B. Lee. 2005. Consequences of mutations in the non-coding RMRP RNA in cartilage-hair hypoplasia. Hum Mol Genet 14:3723-3740.
Bonafe, L., K. Schmitt, G. Eich, A. Giedion, and A. Superti-Furga. 2002. 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 61:146-151.
Yuan, Y., R. Singh, and R. Reddy. 1989. Rat nucleolar 7-2 RNA is homologous to mouse mitochondrial RNase mitochondrial RNA-processing RNA. J Biol Chem 264:14835-14839.
Van Eenennaam, H., J. H. Vogelzangs, D. Lugtenberg, F. H. Van Den Hoogen, W. J. Van Venrooij, and G. J. Pruijn. 2002. Identity of the RNase MRP- and RNase P-associated Th/To autoantigen. Arthritis Rheum 46:3266-3272.
Walker, S. C., and J. M. Avis. 2005. Secondary structure probing of the human RNase MRP RNA reveals the potential for MRP RNA subsets. Biochem Biophys Res Commun 335:314-321.
Welting, T. J., B. J. Kikkert, W. J. van Venrooij, and G. J. Pruijn. 2006. Differential association of protein subunits with the human RNase MRP and RNase P complexes. Rna 12:1373-1382.
Piccinelli, P., M. A. Rosenblad, and T. Samuelsson. 2005. Identification and analysis of ribonuclease P and MRP RNA in a broad range of eukaryotes. Nucleic Acids Res 33:4485-4495.

Human MRP Information:
Schmitt, M. E., J. L. Bennett, D. J. Dairaghi, and D. A. Clayton. 1993. Secondary structure of RNase MRP RNA as predicted by phylogenetic comparison. Faseb J 7:208-213.
van Eenennaam, H., N. Jarrous, W. J. van Venrooij, and G. J. Pruijn. 2000. Architecture and function of the human endonucleases RNase P and RNase MRP. IUBMB Life 49:265-272.
Walker, S. C., and J. M. Avis. 2005. Secondary structure probing of the human RNase MRP RNA reveals the potential for MRP RNA subsets. Biochem Biophys Res Commun 335:314-321.

MRP in other Eukaryotes Information:
Kiss, T., C. Marshallsay, and W. Filipowicz. 1992. 7-2/MRP RNAs in plant and mammalian cells: association with higher order structures in the nucleolus. Embo J 11:3737-3746.
Piccinelli, P., M. A. Rosenblad, and T. Samuelsson. 2005. Identification and analysis of ribonuclease P and MRP RNA in a broad range of eukaryotes. Nucleic Acids Res 33:4485-4495.





















Last update: September 23, 2006 10:12 PM.