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Gene Review

ARR2  -  Arr2p

Saccharomyces cerevisiae S288c

Synonyms: ACR2, Arsenical-resistance protein 2, P9677.16, YPR200C
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Disease relevance of ARR2

  • ACR2 was cloned into a bacterial expression vector and expressed in E. coli as a C-terminally histidine-tagged protein that was purified by sequential metal chelate affinity and gel filtration chromatography [1].

High impact information on ARR2


Chemical compound and disease context of ARR2


Biological context of ARR2

  • The presence of ACR3 together with ACR2 on a multicopy plasmid was conducive to increased arsenate resistance [5].
  • Homology searches revealed a cluster of three new open reading frames named ACR1, ACR2 and ACR3 [6].
  • Substrate specificity as well as sensitivity toward inhibitors for the fern AR (phosphate as a competitive inhibitor, arsenite as a noncompetitive inhibitor) was also similar to Acr2p [7].
  • The yeast Acr2p has an active site motif HC(X)(5)R that is conserved in protein phosphotyrosine phosphatases and rhodanases, suggesting that these three groups of enzymes may have evolved from an ancestral oxyanion-binding protein [8].

Anatomical context of ARR2


Associations of ARR2 with chemical compounds

  • In Saccharomyces cerevisiae, expression of the ACR2 and ACR3 genes confers arsenical resistance [1].
  • In contrast, acr1, acr3, and acr4 mutants were resistant to papulacandin B (an antibiotic containing a disaccharide linked to two fatty acid chains that also inhibits beta-glucan synthesis), but acr2 mutants were susceptible to this antibiotic [11].
  • Acr2p also has a third cysteine residue at position 106 [12].
  • Here we show that creation of a phosphate binding motif through the introduction of glycines at positions 79, 81, and 84 in Acr2p resulted in a gain of phosphotyrosine phosphatase activity and a loss of arsenate reductase activity [13].
  • An arsenate reductase (AR) in the fern showed a reaction mechanism similar to the previously reported Acr2p, an AR from yeast (Saccharomyces cerevisiae), using glutathione as the electron donor [7].

Other interactions of ARR2

  • This suggests that during the catalytic cycle, Acr2p forms a mixed disulfide with GSH before being reduced by glutaredoxin to regenerate the active Acr2p reductase [1].
  • Yap8p is demonstrated to reside in the nucleus where it mediates enhanced expression of the arsenic detoxification genes ACR2 and ACR3 [14].
  • Acr2p is not a phosphatase but is a homologue of CDC25 phosphatases [13].
  • The ACR2 gene of Saccharomyces cerevisiae was disrupted by insertion of a HIS3 gene [10].

Analytical, diagnostic and therapeutic context of ARR2


  1. Purification and characterization of ACR2p, the Saccharomyces cerevisiae arsenate reductase. Mukhopadhyay, R., Shi, J., Rosen, B.P. J. Biol. Chem. (2000) [Pubmed]
  2. Hyperaccumulation of arsenic in the shoots of Arabidopsis silenced for arsenate reductase (ACR2). Dhankher, O.P., Rosen, B.P., McKinney, E.C., Meagher, R.B. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  3. The Transcriptional Response of the Yeast Na+-ATPase ENA1 Gene to Alkaline Stress Involves Three Main Signaling Pathways. Platara, M., Ruiz, A., Serrano, R., Palomino, A., Moreno, F., Ari??o, J. J. Biol. Chem. (2006) [Pubmed]
  4. An arsenate reductase from Synechocystis sp. strain PCC 6803 exhibits a novel combination of catalytic characteristics. Li, R., Haile, J.D., Kennelly, P.J. J. Bacteriol. (2003) [Pubmed]
  5. The Saccharomyces cerevisiae ACR3 gene encodes a putative membrane protein involved in arsenite transport. Wysocki, R., Bobrowicz, P., Ułaszewski, S. J. Biol. Chem. (1997) [Pubmed]
  6. Isolation of three contiguous genes, ACR1, ACR2 and ACR3, involved in resistance to arsenic compounds in the yeast Saccharomyces cerevisiae. Bobrowicz, P., Wysocki, R., Owsianik, G., Goffeau, A., Ułaszewski, S. Yeast (1997) [Pubmed]
  7. Characterization of arsenate reductase in the extract of roots and fronds of Chinese brake fern, an arsenic hyperaccumulator. Duan, G.L., Zhu, Y.G., Tong, Y.P., Cai, C., Kneer, R. Plant Physiol. (2005) [Pubmed]
  8. Arsenate reductases in prokaryotes and eukaryotes. Mukhopadhyay, R., Rosen, B.P. Environ. Health Perspect. (2002) [Pubmed]
  9. Arsenical resistance genes in Saccharomyces douglasii and other yeast species undergo rapid evolution involving genomic rearrangements and duplications. Maciaszczyk, E., Wysocki, R., Golik, P., Lazowska, J., Ulaszewski, S. FEMS Yeast Res. (2004) [Pubmed]
  10. Saccharomyces cerevisiae ACR2 gene encodes an arsenate reductase. Mukhopadhyay, R., Rosen, B.P. FEMS Microbiol. Lett. (1998) [Pubmed]
  11. Isolation and characterization of Saccharomyces cerevisiae mutants resistant to aculeacin A. Font de Mora, J., Gil, R., Sentandreu, R., Herrero, E. Antimicrob. Agents Chemother. (1991) [Pubmed]
  12. The phosphatase C(X)5R motif is required for catalytic activity of the Saccharomyces cerevisiae Acr2p arsenate reductase. Mukhopadhyay, R., Rosen, B.P. J. Biol. Chem. (2001) [Pubmed]
  13. Directed evolution of a yeast arsenate reductase into a protein-tyrosine phosphatase. Mukhopadhyay, R., Zhou, Y., Rosen, B.P. J. Biol. Chem. (2003) [Pubmed]
  14. Transcriptional activation of metalloid tolerance genes in Saccharomyces cerevisiae requires the AP-1-like proteins Yap1p and Yap8p. Wysocki, R., Fortier, P.K., Maciaszczyk, E., Thorsen, M., Leduc, A., Odhagen, A., Owsianik, G., Ulaszewski, S., Ramotar, D., Tamás, M.J. Mol. Biol. Cell (2004) [Pubmed]
  15. Crystallization and preliminary X-ray diffraction analysis of Saccharomyces cerevisiae Ygr203p, a homologue of Acr2 arsenate reductase. Moon, J., Kim, Y.S., Lee, J.Y., Cho, S.J., Song, H.K., Cho, J.H., Kim, B.M., Kim, K.K., Suh, S.W. Acta Crystallogr. D Biol. Crystallogr. (2000) [Pubmed]
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