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Glutathione and gamma‐glutamyl transferases are involved in the formation of cadmium–glutathione complex
Author(s) -
Adamis Paula Daniela Braga,
Mannarino Sérgio Cantú,
Eleutherio Elis Cristina Araújo
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.03.066
Subject(s) - glutathione , cytosol , cadmium , biochemistry , cytoplasm , chemistry , saccharomyces cerevisiae , enzyme , glutathione s transferase , transferase , glutathione reductase , gamma glutamyltransferase , strain (injury) , yeast , biology , organic chemistry , glutathione peroxidase , anatomy
In a wild‐type strain of Saccharomyces cerevisiae , cadmium induces the activities of both gamma‐glutamyl transferase (gamma‐GT) and glutathione transferase 2 (Gtt2). However, Gtt2 activity did not increase under gamma‐GT or Ycf1 deficiencies, suggesting that the accumulation of glutathione–cadmium in the cytosol inhibits Gtt2. On the other hand, the balance between the cytoplasmic and vacuolar level of glutathione seems to regulate gamma‐GT activity, since this enzyme was not activated in a gtt2 strain. Taken together, these results suggest that gamma‐GT and Gtt2 work together to remove cadmium from the cytoplasm, a crucial mechanism for metal detoxification that is dependent on glutathione.