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ALR1  -  Mg(2+) transporter ALR1

Saccharomyces cerevisiae S288c

Synonyms: Aluminum resistance protein 1, Magnesium transporter ALR1, YOL130W
 
 
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High impact information on ALR1

  • The Saccharomyces cerevisiae ALR1 (YOL130w) gene product Alr1p is the first known candidate for a Mg(2+) transport system in eukaryotic cells and is distantly related to the bacterial CorA Mg(2+) transporter family [1].
  • Furthermore, cells lacking the vacuolar protease Pep4p accumulated Alr1p in the vacuole [1].
  • Mutants lacking Alr1p (Deltaalr1) showed a 60% reduction of total intracellular Mg(2+) compared with the wild type and failed to grow in standard media [1].
  • The yeast plasma membrane protein Alr1 controls Mg2+ homeostasis and is subject to Mg2+-dependent control of its synthesis and degradation [1].
  • Yeast strains lacking ALR gene activity required additional Mg2+ for growth, and expression of either ALR1 or ALR2 corrected the Mg(2+)-requiring phenotype [2].
 

Biological context of ALR1

  • Disruption of YOL130w (also known as ALR1) produced a lethal phenotype, despite the presence of a highly similar gene in the yeast genome (ALR2/YFL050C) [3].
  • Random PCR mutagenesis was undertaken of the C-terminal part of ALR1 that is homologous to the bacterial CorA magnesium transport family [4].
 

Anatomical context of ALR1

  • When Mg(2+) was the major cation in the pipette solution, time-dependent outward currents were also detected in CM66+ALR1 protoplasts suggesting ALR1 can facilitate Mg(2+) efflux as well as uptake [5].
 

Associations of ALR1 with chemical compounds

  • The function of Alr1p of Saccharomyces cerevisiae in cadmium detoxification: insights from phylogenetic studies and particle-induced X-ray emission [6].
  • ALR1 is strictly specific for NADPH (2.4 x 10(5) M(-1) s(-1)) whereas ALR2 utilises NADH and NADPH with similar specificity constants of approximately 2-4 x 10(5) M(-1) s(-1) [7].
 

Other interactions of ALR1

  • Two genes in Saccharomyces cerevisiae, ALR1 and ALR2, encode transmembrane proteins involved in Mg2+ uptake [6].
  • Alr1-type proteins are distant relatives of the mitochondrial and bacterial Mg(2+)-transport proteins, Mrs2p and CorA, respectively, with which they have two adjacent TM domains and a short Mg(2+) signature motif in common [8].
 

Analytical, diagnostic and therapeutic context of ALR1

  • The patch-clamp technique was used to measure whole-cell ion currents in protoplasts prepared from the wild-type strain, the alr1 alr2 double mutant (CM66), and the double mutant over-expressing the ALR1 gene (CM66+ALR1) [5].

References

  1. The yeast plasma membrane protein Alr1 controls Mg2+ homeostasis and is subject to Mg2+-dependent control of its synthesis and degradation. Graschopf, A., Stadler, J.A., Hoellerer, M.K., Eder, S., Sieghardt, M., Kohlwein, S.D., Schweyen, R.J. J. Biol. Chem. (2001) [Pubmed]
  2. Overexpression of the Saccharomyces cerevisiae magnesium transport system confers resistance to aluminum ion. MacDiarmid, C.W., Gardner, R.C. J. Biol. Chem. (1998) [Pubmed]
  3. Disruption and phenotypic analysis of seven ORFs from the left arm of chromosome XV of Saccharomyces cerevisiae. Hajji, K., Clotet, J., Ariño, J. Yeast (1999) [Pubmed]
  4. Residues of the yeast ALR1 protein that are critical for magnesium uptake. Lee, J.M., Gardner, R.C. Curr. Genet. (2006) [Pubmed]
  5. Large Mg(2+)-dependent currents are associated with the increased expression of ALR1 in Saccharomyces cerevisiae. Liu, G.J., Martin, D.K., Gardner, R.C., Ryan, P.R. FEMS Microbiol. Lett. (2002) [Pubmed]
  6. The function of Alr1p of Saccharomyces cerevisiae in cadmium detoxification: insights from phylogenetic studies and particle-induced X-ray emission. Kern, A.L., Bonatto, D., Dias, J.F., Yoneama, M.L., Brendel, M., Pêgas Henriques, J.A. Biometals (2005) [Pubmed]
  7. D-Xylose metabolism by Candida intermedia: isolation and characterisation of two forms of aldose reductase with different coenzyme specificities. Mayr, P., Brüggler, K., Kulbe, K.D., Nidetzky, B. J. Chromatogr. B Biomed. Sci. Appl. (2000) [Pubmed]
  8. Oligomerization of the Mg(2+)-transport proteins Alr1p and Alr2p in yeast plasma membrane. Wachek, M., Aichinger, M.C., Stadler, J.A., Schweyen, R.J., Graschopf, A. FEBS J. (2006) [Pubmed]
 
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