Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 114, Issue 31, Pages 8414-8419Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1703344114
Keywords
Nucleoredoxin; Thioredoxin; catalase; oxidative stress; reactive oxygen species
Categories
Funding
- Royal Society [UF090321, UF140600]
- Wellcome Trust-University of Edinburgh [Rg110495]
- European Research Council (ERC) under the European Union [678511]
- Biotechnology and Biological Sciences Research Council (BBSRC)
- Higher Education Commission Pakistan
- BBSRC [BB/D011809/1]
- European Union [602470]
- Centre National de la Recherche Scientifique
- Agence Nationale de la Recherche ANR-Blanc Cynthiol [12-BSV6-0011]
- ISSF award
- Wellcome Trust for the Centre for Immunity, Infection and Evolution [095831/Z/11/Z]
- Wellcome Trust [095831/Z/11/Z] Funding Source: Wellcome Trust
- BBSRC [BB/D011809/1, BB/H000984/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/D011809/1, 1206544, BB/H000984/1] Funding Source: researchfish
- European Research Council (ERC) [678511] Funding Source: European Research Council (ERC)
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Cellular accumulation of reactive oxygen species (ROS) is associated with a wide range of developmental and stress responses. Although cells have evolved to use ROS as signaling 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.
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