López-Mirabal H Reynaldo, Winther Jakob R
Carlsberg Laboratory, Gamle Carlsberg Vej 10, 2500 Copenhagen Valby, Denmark.
Antonie Van Leeuwenhoek. 2007 Nov;92(4):463-72. doi: 10.1007/s10482-007-9174-2. Epub 2007 Jun 13.
Membrane-permeant oxidants have become a standard tool for studying eukaryotic organisms because they affect the redox state and the redox regulation of different compartments. The ero1-1 mutant is temperature sensitive (37 degrees C) and cannot grow under anaerobic conditions. Low micromolar concentrations of the specific thiol-oxidant dipyridyl disulfide (DPS) rescue both these growth defects. Furthermore, the unfolded protein response (UPR) is slightly induced by a DPS treatment. We infer that DPS may change the redox state of important ER-proteins by GSH-oxidation in the ER or, more likely, by directly oxidizing these targets. Therefore, DPS may be useful in genetic studies dealing with unknown factors of the Ero1p-driven pathway. The ero1-1 mutation and the overproduction of Ero1p confer DPS-sensitivity that could be partially related to a more oxidized cytosolic GSH redox potential and the presence of reactive oxidative species (ROS) in the cell.
膜渗透性氧化剂已成为研究真核生物的标准工具，因为它们会影响不同区室的氧化还原状态和氧化还原调节。ero1-1突变体对温度敏感（37摄氏度），在厌氧条件下无法生长。低微摩尔浓度的特定硫醇氧化剂二吡啶二硫化物（DPS）可挽救这两种生长缺陷。此外，DPS处理会轻微诱导未折叠蛋白反应（UPR）。我们推断，DPS可能通过内质网中谷胱甘肽（GSH）的氧化作用，或者更有可能是直接氧化这些靶点，来改变重要内质网蛋白的氧化还原状态。因此，DPS可能有助于处理Ero1p驱动途径中未知因素的遗传学研究。ero1-1突变和Ero1p的过量表达赋予了DPS敏感性，这可能部分与细胞溶质中更氧化的谷胱甘肽氧化还原电位以及细胞中活性氧化物质（ROS）的存在有关。
