RESUMO
Plant annexins function as calcium-dependent or -independent phospholipid binding proteins and constitute about 0.1% of total cellular proteins. Some of them were reported to antagonize oxidative stress and protect plant cells. Brassica juncea annexin-3 (AnnBj3) was recently discovered. To gain insight into a possible function of AnnBj3 in oxidative stress response, we investigated the resistance of Arabidopsis thaliana plants expressing AnnBj3 constitutively. Here we report that, AnnBj3 attenuates methyl viologen-mediated oxidative stress in plants. It protected photosynthesis and plasma membrane from methyl viologen-mediated oxidative damage. AnnBj3 detoxifies hydrogen peroxide and showed antioxidative property in vitro. The protein increased total peroxidase activity in transgenics and interfered with other cellular antioxidants, thereby giving an overall cellular protection against methyl viologen-induced cytotoxicity.
Assuntos
Anexina A3/fisiologia , Arabidopsis/fisiologia , Mostardeira/genética , Estresse Oxidativo , Proteínas de Plantas/fisiologia , Antioxidantes/metabolismo , Homeostase , Paraquat , Peroxidase/metabolismo , Complexo de Proteína do Fotossistema II/metabolismo , Plantas Geneticamente Modificadas/fisiologia , Espécies Reativas de Oxigênio/metabolismoRESUMO
Brassica juncea annexin-3 (BjAnn3) was functionally characterized for its ability to modulate H2O2-mediated oxidative stress in Saccharomyces cerevisiae. BjAnn3 showed a significant protective role in cellular-defense against oxidative stress and partially alleviated inhibition of mitochondrial respiration in presence of exogenously applied H2O2. Heterologous expression of BjAnn3 protected membranes from oxidative stress-mediated damage and positively regulated antioxidant gene expression for ROS detoxification. We conclude that, BjAnn3 partially counteracts the effects of thioredoxin peroxidase 1 (TSA1) deficiency and aids in cellular-protection across kingdoms. Despite partial compensation of TSA1 by BjAnn3 in cell-viability tests, the over-complementation in ROS-related features suggests the existence of both redundant (e.g. ROS detoxification) and distinct features (e.g. membrane protection versus proximity-based redox regulator) of both proteins.