| Abstract |
During exposure of yeast cells to low levels of hydrogen peroxide (H2O2), the expression of several genes is regulated for cells to adapt to the surrounding oxidative environment. Such adaptation involves modification of plasma membrane lipid composition, reorganization of ergosterol-rich microdomains and altered gene expression of proteins involved in lipid and vesicle traffic, to decrease permeability to exogenous H2O2. Opi1p is a transcriptional repressor that is inactive when present at the nuclear membrane/endoplasmic reticulum, but represseses transcription of inositol upstream activating sequence (UAS(INO))-containing genes, many of which are involved in the synthesis of phospholipids and fatty acids, when it is translocated to the nucleus. We investigated whether H2O2 in concentrations inducing adaptation regulates Opi1p function. We found that, in the presence of H2O2, GFP-Opi1p fusion protein translocates to the nucleus and, concomitantly, the expression of UAS(INO)-containing genes is affected. We also investigated whether cysteine residues of Opi1p were implicated in the H2O2-mediated translocation of this protein to the nucleus and identified cysteine residue 159 as essential for this process. Our work shows that Opi1p is redox-regulated and establishes a new mechanism of gene regulation involving Opi1p, which is important for adaptation to H2O2 in yeast cells. Copyright (c) 2017 John Wiley \& Sons, Ltd. |
