Functional switching of ascorbate peroxidase 2 of rice (OsAPX2) between peroxidase and molecular chaperone.

Ascorbate peroxidase (APX) is a class I haem-containing peroxidase, which catalyses the conversion of HO to HO and O using ascorbate as the specific electron donor. APX plays a central role in the elimination of intracellular reactive oxygen species (ROS) and protects plants from the oxidative damage that can occur as a result of biotic and abiotic stresses. At present, the only known function of APX is as a peroxidase. However, in this study, we demonstrate that Oryza sativa APX2 also operates as a molecular chaperone in rice. The different functions of OsAPX2 correlate strongly with its structural conformation. The high-molecular-weight (HMW) complexes had chaperone activity, whereas the low-molecular-weight (LMW) forms displayed predominantly APX activity. The APX activity was effectively inhibited by sodium azide, which is an inhibitor of haem-containing enzymes, but this did not affect the protein's activity as a chaperone. Additionally, the OsAPX2 conformational changes could be regulated by salt and heat stresses and these stimulated OsAPX2 dissociation and association, respectively. Our results provide new insight into the roles of APXs.