668 / 2019-04-30 15:00:43

Redox-Dependent Chaperone function of Universal Stress Protein Enhances Heat Shock and Oxidative Stress Tolerance in Arabidopsis

redox,Oxidative stress,heat stress

全体主题 > Abiotic Stress

Molecular and biochemical functions of Universal Stress Proteins (USPs) remain unidentified in plant, and this study investigated the biochemical function of AtUSP (At3g53990) in Arabidopsis thaliana. AtUSP over-expressing plants enhanced a heat shock and oxidative stress tolerance compared with wild-type and atusp knock-out plants. AtUSP protein was composed with a high molecular weight (HMW) oligomeric complexes and a low molecular weight (LMW) including monomers, dimers and trimers. Interestingly, AtUSP switched its structure from LMW species to HMW complexes in response to heat shock and oxidative stress. Chaperone activity of AtUSP was significantly increased by heat shock and the activity was critically regulated by the redox status, followed by structural switches of the protein. redox-dependent chaperone activity leads to enhanced a tolerance to heat shock and oxidative stress of over-expression of AtUSP accompanied by a structural switch from LMW to HMW.