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Gene Review

MRS6  -  Mrs6p

Saccharomyces cerevisiae S288c

Synonyms: MSI4, REP, Rab escort protein, Rab proteins geranylgeranyltransferase component A, YOR370C
 
 
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Disease relevance of MRS6

  • The yeast MRS6 gene encodes a protein that is approximately 30% identical to the choroideremia gene product [1].
 

High impact information on MRS6

  • We propose that the REP loci constitute a copy control system that overrides normal cellular restriction on plasmid replication and amplifies the plasmid when copy number is low [2].
  • Rab escort proteins (REP) 1 and 2 are closely related mammalian proteins required for prenylation of newly synthesized Rab GTPases by the cytosolic heterodimeric Rab geranylgeranyl transferase II complex (RabGG transferase) [3].
  • Although REP and GDI share common Rab-binding properties, GDI cannot assist in Rab prenylation and REP cannot retrieve Rab proteins from the membranes [4].
  • After delivery to the membrane by the REP-Rab complex, subsequent recycling to the cytosol requires the REP-related guanine-nucleotide-dissociation-inhibitor (GDI) [4].
  • Molecular evolution of the Rab-escort-protein/guanine-nucleotide-dissociation-inhibitor superfamily [4].
 

Biological context of MRS6

  • The only known yeast homologue of the choroideremia gene product is encoded by an essential gene called MRS6 [5].
  • Disruption of the MRS6 gene is lethal to haploid yeast cells [6].
  • Unexpectedly, the MRS6 gene product also affects mitochondrial functions as revealed by the facts that high-copy numbers of MRS6 (1) suppress the pet- phenotype of mrs2-1 mutant strains and (2) cause a weak pet- phenotype in wild-type strains [6].
  • Here, we report the characterization of a yeast REP mutant, mrs6-2, in which reduced prenylation of Ypt proteins occurs even at the permissive temperature [7].
  • A gene disruption experiment showed that MSI4 is essential for cell growth [8].
 

Anatomical context of MRS6

 

Associations of MRS6 with chemical compounds

  • A point mutant allele of AthREP with arginine at this position complemented the yeast REP mutation, while wild-type AthREP did not [10].
  • We found that a conserved arginine residue, R195, known to be crucial for yeast REP function, is substituted by an asparagine or threonine residue in angiosperm REPs [10].
  • Prenylated Ypt1p obtained after incubation of Ypt1p with PGGTase-II, Msi4p, and geranylgeranyl diphosphate was digested with trypsin [11].
  • Recombinant Msi4p with an N-terminal polyhistidine leader was purified on a Ni(2+)-Sepharose column, followed by gel filtration and ion exchange chromatography [11].
  • In yeast estrogen receptor transcription assay, both EEP and REP were found to be estrogenic with EC(50) values of 9.48, and 8.55 microg/ml, respectively [12].
 

Regulatory relationships of MRS6

  • Here we characterize an antiserum directed against Mrs6p and show that it specifically inhibits the geranylation of the YPT1 protein in an in vitro assay [13].
 

Other interactions of MRS6

  • To investigate its functions further, we constructed a strain whose MSI4 is driven by the GAL1 promoter [8].
  • We describe the isolation of MSI4 as a multicopy suppressor of ira1 (inhibitory regulator of Ras) [8].
 

Analytical, diagnostic and therapeutic context of MRS6

  • We used oligonucleotide primers that are complementary to (i) intron splice sites, (ii) REP and (iii) ERIC elements to produce PCR fingerprints that display specific patterns between the different yeast species [14].

References

  1. Identification of yeast component A: reconstitution of the geranylgeranyltransferase that modifies Ypt1p and Sec4p. Jiang, Y., Ferro-Novick, S. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  2. The yeast plasmid 2mu circle encodes components required for its high copy propagation. Jayaram, M., Li, Y.Y., Broach, J.R. Cell (1983) [Pubmed]
  3. Molecular basis for Rab prenylation. Alory, C., Balch, W.E. J. Cell Biol. (2000) [Pubmed]
  4. Molecular evolution of the Rab-escort-protein/guanine-nucleotide-dissociation-inhibitor superfamily. Alory, C., Balch, W.E. Mol. Biol. Cell (2003) [Pubmed]
  5. Amino- and carboxy-terminal domains of the yeast Rab escort protein are both required for binding of Ypt small G proteins. Bauer, B.E., Lorenzetti, S., Miaczynska, M., Bui, D.M., Schweyen, R.J., Ragnini, A. Mol. Biol. Cell (1996) [Pubmed]
  6. The yeast protein Mrs6p, a homologue of the rabGDI and human choroideraemia proteins, affects cytoplasmic and mitochondrial functions. Ragnini, A., Teply, R., Waldherr, M., Voskova, A., Schweyen, R.J. Curr. Genet. (1994) [Pubmed]
  7. Low levels of Ypt protein prenylation cause vesicle polarization defects and thermosensitive growth that can be suppressed by genes involved in cell wall maintenance. Bialek-Wyrzykowska, U., Bauer, B.E., Wagner, W., Kohlwein, S.D., Schweyen, R.J., Ragnini, A. Mol. Microbiol. (2000) [Pubmed]
  8. The Saccharomyces cerevisiae MSI4 gene encodes the yeast counterpart of component A of Rab geranylgeranyltransferase. Fujimura, K., Tanaka, K., Nakano, A., Toh-e, A. J. Biol. Chem. (1994) [Pubmed]
  9. The yeast Rab escort protein binds intracellular membranes in vivo and in vitro. Miaczynska, M., Lorenzetti, S., Bialek, U., Benito-Moreno, R.M., Schweyen, R.J., Ragnini, A. J. Biol. Chem. (1997) [Pubmed]
  10. A specific feature of the angiosperm Rab escort protein (REP) and evolution of the REP/GDI superfamily. Hála, M., Eliás, M., Zárský, V. J. Mol. Biol. (2005) [Pubmed]
  11. Yeast geranylgeranyltransferase type-II: steady state kinetic studies of the recombinant enzyme. Witter, D.J., Poulter, C.D. Biochemistry (1996) [Pubmed]
  12. Estrogenic effects of ethanol and ether extracts of propolis. Song, Y.S., Jin, C., Jung, K.J., Park, E.H. Journal of ethnopharmacology. (2002) [Pubmed]
  13. Mrs6p, the yeast homologue of the mammalian choroideraemia protein: immunological evidence for its function as the Ypt1p Rab escort protein. Benito-Moreno, R.M., Miaczynska, M., Bauer, B.E., Schweyen, R.J., Ragnini, A. Curr. Genet. (1994) [Pubmed]
  14. New PCR-based methods for yeast identification. Hierro, N., González, A., Mas, A., Guillamón, J.M. J. Appl. Microbiol. (2004) [Pubmed]
 
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