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RPM2  -  Rpm2p

Saccharomyces cerevisiae S288c

Synonyms: RNase P, Ribonuclease P protein component, mitochondrial, YML091C
 
 
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Disease relevance of RPM2

  • Both are substrates for E. coli RNase P. Partial nuclease digestions show that the tRNA portions of the two precursors differ in tertiary structure, while their 5' leaders differ in secondary structure [1].
  • Buoyant density and relative molecular mass of cyanelle RNase P were more similar to the eukaryotic (nuclear or mitochondrial) than to the bacterial enzyme type, despite the close phylogenetic relationship between plastids and cyanobacteria [2].
  • We investigated the catalytic efficiency and the specificity of the Bacillus subtilis RNase P holoenzyme reaction with substrates that contain a single strand, a hairpin loop, or a tRNA 3' to the cleavage site [3].
 

High impact information on RPM2

 

Chemical compound and disease context of RPM2

  • The 5'-terminal guanylate residue (G-1) of mature Escherichia coli tRNA(His) is generated as a result of an unusual cleavage by RNase P (Orellana, O., Cooley, L., and Söll, D. (1986) Mol. Cell. Biol. 6, 525-529) [8].
  • The cleavage specificities of the RNase P holoenzymes from Escherichia coli and the yeast Schizosaccharomyces pombe and of the catalytic M1 RNA from E. coli were analyzed in 5'-processing experiments using a yeast serine pre-tRNA with mutations in both flanking sequences [9].
  • The phosphorothioate footprinting technique was applied to the investigation of phosphate moieties in tRNA substrates involved in interactions with M1 RNA, the catalytic subunit of Escherichia coli RNase P. In general agreement with previous data, all affected sites were localized in acceptor stem and T arm [10].
 

Biological context of RPM2

  • The ability of RPM2 alleles to suppress tom40-3, a temperature-sensitive mutant of a component of the mitochondrial import apparatus, correlates with their ability to transactivate the reporter genes with lexA-binding sites [11].
  • We report here that alteration in the biogenesis of Rpm1r, the RNase P RNA subunit, is another consequence of disrupting RPM2 [12].
  • We report here that if strains containing the truncated RPM2 allele are created and maintained on respiratory carbon sources they have wild-type mitochondrial genomes, and a significant portion of tRNA transcripts are processed [13].
  • RPM2 is a Saccharomyces cerevisiae nuclear gene required for normal cell growth yet the only known function of Rpm2p is as a protein subunit of yeast mitochondrial RNase P, an enzyme responsible for the 5' maturation of mitochondrial tRNAs [14].
  • The transcriptional activation region of Rpm2p contains two leucine zippers that are required for transcriptional activation and are conserved in the distantly related yeast Candida glabrata [11].
 

Anatomical context of RPM2

  • RNase P from the mitochondria of Saccharomyces cerevisiae was purified to near homogeneity > 1800-fold with a yield of 1.6% from mitochondrial extracts [15].
  • The ubiquitous RNase P RNP, which has a single protein component in Bacteria and Archaea, requires at least two protein subunits for its function in eukaryotic cells [16].
 

Associations of RPM2 with chemical compounds

  • Previous work demonstrated that an insertional disruption of RPM2, which produces the C-terminally truncated protein Rpm2-DeltaCp, supports growth on glucose but cells lose some or all of their mitochondrial genome and become petite [13].
  • An RNA of 227 nucleotides that is one of the RNAs encoded by the gene that we mapped cofractionated with this mitochondrial RNase P activity on glycerol gradients [17].
  • A single base change in the intron of a serine tRNA affects the rate of RNase P cleavage in vitro and suppressor activity in vivo in Saccharomyces cerevisiae [18].
  • Processing of histidine transfer RNA precursors. Abnormal cleavage site for RNase P [8].
  • (p denotes a [32P]phosphate group.) This substrate was cleaved by yeast RNase P to the mature tRNA and a tetranucleoside triphosphate ApApApCOH [19].
 

Physical interactions of RPM2

 

Regulatory relationships of RPM2

  • A Val-to-Phe substitution within a highly conserved region of Pre4p that disrupts proteasome function suppresses the growth arrest of RPM2-null cells on fermentable media [21].
 

Other interactions of RPM2

  • The SEF1 homologue of S. cerevisiae also compensates for the essential function of RPM2 [14].
  • RPM2 is identified here as a high-copy suppressor of isp42-3, a temperature-sensitive mutant allele of the mitochondrial protein import channel component, Isp42p [22].
  • Sequence analysis revealed that most of the remaining regulated fusions are in new yeast genes, while some are in previously characterized yeast genes (PTP1, RPM2, SDH1) [23].
  • Our results suggest that Hap2p could play a more general role by regulating other mitochondrial processes such as protein import and phosphate transport (PTP1) or maturation of mitochondrial tRNAs (RPM2) [23].
  • More importantly, we show that a novel class of repression modules-RPM1, encompassing residues 245 to 278; RPM2, encompassing residues 1061 to 1185; and RPM3, encompassing residues 203 to 244-is critical for Hap1 repression in the absence of heme [24].
 

Analytical, diagnostic and therapeutic context of RPM2

References

  1. Alteration of a mitochondrial tRNA precursor 5' leader abolishes its cleavage by yeast mitochondrial RNase P. Hollingsworth, M.J., Martin, N.C. Nucleic Acids Res. (1987) [Pubmed]
  2. Cyanelle RNase P: RNA structure analysis and holoenzyme properties of an organellar ribonucleoprotein enzyme. Cordier, A., Schön, A. J. Mol. Biol. (1999) [Pubmed]
  3. The 3' substrate determinants for the catalytic efficiency of the Bacillus subtilis RNase P holoenzyme suggest autolytic processing of the RNase P RNA in vivo. Loria, A., Pan, T. RNA (2000) [Pubmed]
  4. Purification and characterization of the nuclear RNase P holoenzyme complex reveals extensive subunit overlap with RNase MRP. Chamberlain, J.R., Lee, Y., Lane, W.S., Engelke, D.R. Genes Dev. (1998) [Pubmed]
  5. Nucleolar localization of early tRNA processing. Bertrand, E., Houser-Scott, F., Kendall, A., Singer, R.H., Engelke, D.R. Genes Dev. (1998) [Pubmed]
  6. The POP1 gene encodes a protein component common to the RNase MRP and RNase P ribonucleoproteins. Lygerou, Z., Mitchell, P., Petfalski, E., Séraphin, B., Tollervey, D. Genes Dev. (1994) [Pubmed]
  7. Identification and characterization of an RNA molecule that copurifies with RNase P activity from HeLa cells. Bartkiewicz, M., Gold, H., Altman, S. Genes Dev. (1989) [Pubmed]
  8. Processing of histidine transfer RNA precursors. Abnormal cleavage site for RNase P. Burkard, U., Willis, I., Söll, D. J. Biol. Chem. (1988) [Pubmed]
  9. Sequence changes in both flanking sequences of a pre-tRNA influence the cleavage specificity of RNase P. Krupp, G., Kahle, D., Vogt, T., Char, S. J. Mol. Biol. (1991) [Pubmed]
  10. Differences in the interaction of Escherichia coli RNase P RNA with tRNAs containing a short or a long extra arm. Gaur, R.K., Hanne, A., Conrad, F., Kahle, D., Krupp, G. RNA (1996) [Pubmed]
  11. Rpm2p, a component of yeast mitochondrial RNase P, acts as a transcriptional activator in the nucleus. Stribinskis, V., Heyman, H.C., Ellis, S.R., Steffen, M.C., Martin, N.C. Mol. Cell. Biol. (2005) [Pubmed]
  12. Yeast mitochondrial RNase P RNA synthesis is altered in an RNase P protein subunit mutant: insights into the biogenesis of a mitochondrial RNA-processing enzyme. Stribinskis, V., Gao, G.J., Sulo, P., Dang, Y.L., Martin, N.C. Mol. Cell. Biol. (1996) [Pubmed]
  13. Rpm2p: separate domains promote tRNA and Rpm1r maturation in Saccharomyces cerevisiae mitochondria. Stribinskis, V., Gao, G.J., Sulo, P., Ellis, S.R., Martin, N.C. Nucleic Acids Res. (2001) [Pubmed]
  14. Kluyveromyces lactis SEF1 and its Saccharomyces cerevisiae homologue bypass the unknown essential function, but not the mitochondrial RNase P function, of the S. cerevisiae RPM2 gene. Groom, K.R., Heyman, H.C., Steffen, M.C., Hawkins, L., Martin, N.C. Yeast (1998) [Pubmed]
  15. A 105-kDa protein is required for yeast mitochondrial RNase P activity. Morales, M.J., Dang, Y.L., Lou, Y.C., Sulo, P., Martin, N.C. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  16. Pop3p is essential for the activity of the RNase MRP and RNase P ribonucleoproteins in vivo. Dichtl, B., Tollervey, D. EMBO J. (1997) [Pubmed]
  17. A gene required for RNase P activity in Candida (Torulopsis) glabrata mitochondria codes for a 227-nucleotide RNA with homology to bacterial RNase P RNA. Shu, H.H., Wise, C.A., Clark-Walker, G.D., Martin, N.C. Mol. Cell. Biol. (1991) [Pubmed]
  18. A single base change in the intron of a serine tRNA affects the rate of RNase P cleavage in vitro and suppressor activity in vivo in Saccharomyces cerevisiae. Willis, I., Frendewey, D., Nichols, M., Hottinger-Werlen, A., Schaack, J., Söll, D. J. Biol. Chem. (1986) [Pubmed]
  19. Partial purification of RNase P from Schizosaccharomyces pombe. Kline, L., Nishikawa, S., Söll, D. J. Biol. Chem. (1981) [Pubmed]
  20. Rpm2p, a protein subunit of mitochondrial RNase P, physically and genetically interacts with cytoplasmic processing bodies. Stribinskis, V., Ramos, K.S. Nucleic Acids Res. (2007) [Pubmed]
  21. Proteasome mutants, pre4-2 and ump1-2, suppress the essential function but not the mitochondrial RNase P function of the Saccharomyces cerevisiae gene RPM2. Lutz, M.S., Ellis, S.R., Martin, N.C. Genetics (2000) [Pubmed]
  22. RPM2, independently of its mitochondrial RNase P function, suppresses an ISP42 mutant defective in mitochondrial import and is essential for normal growth. Kassenbrock, C.K., Gao, G.J., Groom, K.R., Sulo, P., Douglas, M.G., Martin, N.C. Mol. Cell. Biol. (1995) [Pubmed]
  23. A genetic screen to isolate genes regulated by the yeast CCAAT-box binding protein Hap2p. Dang, V.D., Valens, M., Bolotin-Fukuhara, M., Daignan-Fornier, B. Yeast (1994) [Pubmed]
  24. A new class of repression modules is critical for heme regulation of the yeast transcriptional activator Hap1. Hach, A., Hon, T., Zhang, L. Mol. Cell. Biol. (1999) [Pubmed]
  25. Yeast mitochondrial RNase P. Sequence of the RPM2 gene and demonstration that its product is a protein subunit of the enzyme. Dang, Y.L., Martin, N.C. J. Biol. Chem. (1993) [Pubmed]
  26. Protein-protein interactions with subunits of human nuclear RNase P. Jiang, T., Altman, S. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  27. Successful transformation of yeast mitochondria with RPM1: an approach for in vivo studies of mitochondrial RNase P RNA structure, function and biosynthesis. Sulo, P., Groom, K.R., Wise, C., Steffen, M., Martin, N. Nucleic Acids Res. (1995) [Pubmed]
 
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