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Gene Review

MET22  -  Met22p

Saccharomyces cerevisiae S288c

Synonyms: 3'(2'),5'-bisphosphate nucleotidase, 3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase, DPNPase, HAL2, Halotolerance protein HAL2, ...
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Disease relevance of MET22

  • The recent visualization at the atomic level of the inhibitory site of sodium in the known target Hal2 has helped identify the interactions determining Na(+) toxicity [1].
  • This protein is homologous to the HAL2 and CysQ phosphatases of yeast and Escherichia coli, respectively [2].

High impact information on MET22


Chemical compound and disease context of MET22

  • X-ray structure of yeast Hal2p, a major target of lithium and sodium toxicity, and identification of framework interactions determining cation sensitivity [6].

Biological context of MET22

  • The substrate specificity and kinetics of RHL enzyme are very similar to the Chlorella 3'(2'),5'-diphosphonucleoside 3'(2')-phosphohydrolase (DPNPase) [7].
  • We used a biochemical genomics approach to identify two yeast phosphatases that can convert Appr1p to ADP-ribose: the product of ORF YBR022w (now Poa1p), which is completely unrelated to other known phosphatases; and Hal2p, a known 3'-phosphatase of 5',3'-pAp [8].

Associations of MET22 with chemical compounds


Other interactions of MET22

  • We have shown that yeast cells can better adapt to the presence of sodium than lithium because of their ability to reduce pAp accumulation by activating HAL2 expression in a Gcn4p-dependent response, a regulatory loop that is likely to be conserved in different yeast species [9].

Analytical, diagnostic and therapeutic context of MET22


  1. Ion homeostasis during salt stress in plants. Serrano, R., Rodriguez-Navarro, A. Curr. Opin. Cell Biol. (2001) [Pubmed]
  2. The SAL1 gene of Arabidopsis, encoding an enzyme with 3'(2'),5'-bisphosphate nucleotidase and inositol polyphosphate 1-phosphatase activities, increases salt tolerance in yeast. Quintero, F.J., Garciadeblás, B., Rodríguez-Navarro, A. Plant Cell (1996) [Pubmed]
  3. A salt-sensitive 3'(2'),5'-bisphosphate nucleotidase involved in sulfate activation. Murguía, J.R., Bellés, J.M., Serrano, R. Science (1995) [Pubmed]
  4. Lithium toxicity in yeast is due to the inhibition of RNA processing enzymes. Dichtl, B., Stevens, A., Tollervey, D. EMBO J. (1997) [Pubmed]
  5. Salt tolerance and methionine biosynthesis in Saccharomyces cerevisiae involve a putative phosphatase gene. Gläser, H.U., Thomas, D., Gaxiola, R., Montrichard, F., Surdin-Kerjan, Y., Serrano, R. EMBO J. (1993) [Pubmed]
  6. X-ray structure of yeast Hal2p, a major target of lithium and sodium toxicity, and identification of framework interactions determining cation sensitivity. Albert, A., Yenush, L., Gil-Mascarell, M.R., Rodriguez, P.L., Patel, S., Martínez-Ripoll, M., Blundell, T.L., Serrano, R. J. Mol. Biol. (2000) [Pubmed]
  7. A rice HAL2-like gene encodes a Ca(2+)-sensitive 3'(2'),5'-diphosphonucleoside 3'(2')-phosphohydrolase and complements yeast met22 and Escherichia coli cysQ mutations. Peng, Z., Verma, D.P. J. Biol. Chem. (1995) [Pubmed]
  8. A highly specific phosphatase that acts on ADP-ribose 1''-phosphate, a metabolite of tRNA splicing in Saccharomyces cerevisiae. Shull, N.P., Spinelli, S.L., Phizicky, E.M. Nucleic Acids Res. (2005) [Pubmed]
  9. Sodium-induced GCN4 expression controls the accumulation of the 5' to 3' RNA degradation inhibitor, 3'-phosphoadenosine 5'-phosphate. Todeschini, A.L., Condon, C., Bénard, L. J. Biol. Chem. (2006) [Pubmed]
  10. Definition of a metal-dependent/Li(+)-inhibited phosphomonoesterase protein family based upon a conserved three-dimensional core structure. York, J.D., Ponder, J.W., Majerus, P.W. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  11. The yeast HAL2 nucleotidase is an in vivo target of salt toxicity. Murguía, J.R., Bellés, J.M., Serrano, R. J. Biol. Chem. (1996) [Pubmed]
  12. Molecular cloning and biochemical characterization of a 3'(2'),5'-bisphosphate nucleotidase from Debaryomyces hansenii. Aggarwal, M., Bansal, P.K., Mondal, A.K. Yeast (2005) [Pubmed]
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