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MRP2  -  mitochondrial 37S ribosomal protein MRP2

Saccharomyces cerevisiae S288c

Synonyms: 37S ribosomal protein MRP2, mitochondrial, P9325.7, YPR166C
 
 
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Disease relevance of MRP2

  • MRP2 codes for a 14-kDa polypeptide homologous to protein S14 of the Escherichia coli small ribosomal subunit and to a chloroplast-encoded component of chloroplast ribosomes [1].
  • Mammalian cells transfected with MRP1 or MRP2 were resistant to GSAO, whereas cells transfected with MRP3, MRP4, MRP5, P-glypoprotein, or breast cancer resistance protein were not [2].
 

High impact information on MRP2

  • Because of the structural and functional homology between Ycf1p and MRP1 and MRP2, these data support the hypothesis that GSH efflux from mammalian cells is mediated by these membrane proteins [3].
  • Assembly of the mitochondrial membrane system. MRP1 and MRP2, two yeast nuclear genes coding for mitochondrial ribosomal proteins [1].
  • The wild type genes MRP1 and MRP2 were cloned by transformation of the pet mutations in E795 and C167, respectively, with a recombinant plasmid library of wild type yeast genomic DNA [1].
  • Transcript mapping revealed at least 111 base pairs within the RHO1-MRP2 intercoding region are transcribed in both directions [4].
  • The results indicate that the kinetics of excretion of alkylphenol-glucuronides into the bile or vein depends on the length of alkyl chain and suggest that nonylphenol-glucuronide formed in the liver cannot be transported by MRP-2 [5].
 

Biological context of MRP2

 

Anatomical context of MRP2

  • Determination of phase I metabolic enzyme activities in liver microsomes of Mrp2 deficient TR- and EHBR rats [7].
 

Associations of MRP2 with chemical compounds

 

Other interactions of MRP2

  • Incorporation of the yeast mitochondrial ribosomal protein Mrp2 into ribosomal subunits requires the mitochondrially encoded Var1 protein [6].

References

  1. Assembly of the mitochondrial membrane system. MRP1 and MRP2, two yeast nuclear genes coding for mitochondrial ribosomal proteins. Myers, A.M., Crivellone, M.D., Tzagoloff, A. J. Biol. Chem. (1987) [Pubmed]
  2. Mechanism of selectivity of an angiogenesis inhibitor from screening a genome-wide set of Saccharomyces cerevisiae deletion strains. Dilda, P.J., Don, A.S., Tanabe, K.M., Higgins, V.J., Allen, J.D., Dawes, I.W., Hogg, P.J. J. Natl. Cancer Inst. (2005) [Pubmed]
  3. ATP-dependent transport of reduced glutathione on YCF1, the yeast orthologue of mammalian multidrug resistance associated proteins. Rebbeor, J.F., Connolly, G.C., Dumont, M.E., Ballatori, N. J. Biol. Chem. (1998) [Pubmed]
  4. Functional analysis of mRNA 3' end formation signals in the convergent and overlapping transcription units of the S. cerevisiae genes RHO1 and MRP2. Peterson, J.A., Myers, A.M. Nucleic Acids Res. (1993) [Pubmed]
  5. Glucuronidation and excretion of nonylphenol in perfused rat liver. Daidoji, T., Inoue, H., Kato, S., Yokota, H. Drug Metab. Dispos. (2003) [Pubmed]
  6. Incorporation of the yeast mitochondrial ribosomal protein Mrp2 into ribosomal subunits requires the mitochondrially encoded Var1 protein. Davis, S.C., Ellis, S.R. Mol. Gen. Genet. (1995) [Pubmed]
  7. Determination of phase I metabolic enzyme activities in liver microsomes of Mrp2 deficient TR- and EHBR rats. Newton, D.J., Wang, R.W., Evans, D.C. Life Sci. (2005) [Pubmed]
  8. ATP-dependent transport of reduced glutathione in yeast secretory vesicles. Rebbeor, J.F., Connolly, G.C., Dumont, M.E., Ballatori, N. Biochem. J. (1998) [Pubmed]
 
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