Endoplasmic reticulum stress triggers ROS signalling, changes the redox state, and regulates the antioxidant defence of Arabidopsis thaliana.

ABSTRACT: Inefficient chaperone activity in endoplasmic reticulum (ER) causes accumulation of unfolded proteins and is called ER stress, which triggers the unfolded protein response. For proper oxidative protein folding, reactive oxygen species (ROS) such as H2O2 are produced in the ER. Although the role of ROS during abiotic stresses such as salinity is well documented, the role of ER-related ROS production and its signalling is not yet known. Moreover, how H2O2 production, redox regulation, and antioxidant defence are affected in salt-treated plants when ER protein-folding machinery is impaired needs to be elucidated. For this aim, changes in NADPH-oxidase-dependent ROS signalling and H2O2 content at sequential time intervals and after 48 h of ER stress, induced by tunicamycin (Tm), salinity, and

SUBMITTER: Ozgur R 

PROVIDER: S-EPMC3969530 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature