An investigation on the relation between endoplasmic reticulum stress and reactive oxygen species in Arabidopsis under some environmental stresses

Accumulation of unfolded proteins caused by inefficient chaperone activity in 'Endoplasmic Reticulum' under salinity and osmotic stresses is called 'Endoplasmic Reticulum Stress'. Under normal condition, this stress can be induced by heavy secretory protein pathway load. On the other hand, exogenous application of antibiotic tunicamycin -which inhibits protein folding- can also induce ER stress artificially. Increase in gene expression due to ER stress induces a response called 'Unfolded Protein Response', which increases protein folding capacity and induces some responses that alleviate ER stress. Formation of disulfide bonds, which are produced by using molecular oxygen, is needed for correct protein folding. As a result of this process, reactive oxygen species (ROS) such as H2O2 is produced in ER. Increased production of ROS results in oxidative damage in cells. Plants have enzymatic and non-enzymatic antioxidant systems to prevent oxidative damage which is produced by ROS. Considering this gap in the literature, we aimed to investigate the organaller production of ROS, in mitochondria, chloroplast and peroxisomes and the effect of this ROS on antioxidant defense system and redox state in these compartments during "ER stress" and "Unfolded Protein Response".