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

ABSTRACT: Ascorbate peroxidase (APX) is a class I haem-containing peroxidase, which catalyses the conversion of H2O2 to H2O and O2 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 effec

SUBMITTER: Hong SH 

PROVIDER: S-EPMC6003922 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature