Nucleoredoxin guards against oxidative stress by protecting antioxidant enzymes

Cellular accumulation of reactive oxygen species (ROS) is associated with a wide range of developmental and stress responses. While cells have evolved to utilise ROS as signalling molecules, their chemically reactive nature also poses a threat. Antioxidant systems are required to detoxify ROS and prevent cellular damage, but little is known about how these systems manage to function in hostile, ROS-rich environments. Here we show that during oxidative stress in plant cells, the pathogen-inducible oxidoreductase, Nucleoredoxin 1 (NRX1), targets enzymes of major hydrogen peroxide (H2O2) scavenging pathways, including catalases. Mutant nrx1 plants displayed reduced catalase activity and were hypersensitive to oxidative stress. Remarkably, catalase was maintained in a reduced state by substrate-interaction with NRX1, a process necessary for its H2O2 scavenging activity. These data suggest that unexpectedly H2O2 scavenging enzymes experience oxidative distress in ROS-rich environments and require reductive protection from NRX1 for optimal activity.