TY - JOUR AU - Chi, Yong Hun AU - Paeng, Seol Ki AU - Kim, Min Ji AU - Hwang, Gwang Yong AU - Melencion, Sarah Mae AU - Oh, Hun Taek AU - Lee, Sang Yeol PY - 2013 M3 - Review TI - Redox-dependent functional switching of plant proteins accompanying with their structural changes JO - Frontiers in Plant Science UR - https://www.frontiersin.org/articles/10.3389/fpls.2013.00277 VL - 4 SN - 1664-462X N2 - Reactive oxygen species (ROS) can be generated during the course of normal aerobic metabolism or when an organism is exposed to a variety of stress conditions. It can cause a widespread damage to intracellular macromolecules and play a causal role in many degenerative diseases. Like other aerobic organisms plants are also equipped with a wide range of antioxidant redox proteins, such as superoxide dismutase, catalase, glutaredoxin, thioredoxin (Trx), Trx reductase, protein disulfide reductase, and other kinds of peroxidases that are usually significant in preventing harmful effects of ROS. To defend plant cells in response to stimuli, a part of redox proteins have shown to play multiple functions through the post-translational modification with a redox-dependent manner. For the alternative switching of their cellular functions, the redox proteins change their protein structures from low molecular weight to high molecular weight (HMW) protein complexes depending on the external stress. The HMW proteins are reported to act as molecular chaperone, which enable the plants to enhance their stress tolerance. In addition, some transcription factors and co-activators have function responding to environmental stresses by redox-dependent structural changes. This review describes the molecular mechanism and physiological significance of the redox proteins, transcription factors and co-activators to protect the plants from environmental stresses through the redox-dependent structural and functional switching of the plant redox proteins. ER -