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Updated: May 2, 2026

Analysis of Oxidative Stress in Zebrafish Embryos
Published on: July 7, 2014
Superoxide dismutase 1 acts as a nuclear transcription factor to regulate oxidative stress resistance
Chi Kwan Tsang1, Yuan Liu2, Janice Thomas1
11] Rutgers Cancer Institute of New Jersey, Rutgers, the State University of New Jersey, New Brunswick, New Jersey 08903, USA [2] Department of Pharmacology, Robert Wood Johnson Medical School (RWJMS), Rutgers, the State University of New Jersey, 195 Little Albany Street, New Brunswick, New Jersey 08903, USA.
Abstract:
Superoxide dismutase 1 (Sod1) has been known for nearly half a century for catalysis of superoxide to hydrogen peroxide. Here we report a new Sod1 function in oxidative signalling: in response to elevated endogenous and exogenous reactive oxygen species (ROS), Sod1 rapidly relocates into the nucleus, which is important for maintaining genomic stability. Interestingly, H2O2 is sufficient to promote Sod1 nuclear localization, indicating that it is responding to general ROS rather than Sod1 substrate superoxide. ROS signalling is mediated by Mec1/ATM and its effector Dun1/Cds1 kinase, through Dun1 interaction with Sod1 and regulation of Sod1 by phosphorylation at S60, 99. In the nucleus, Sod1 binds to promoters and regulates the expression of oxidative resistance and repair genes. Altogether, our study unravels an unorthodox function of Sod1 as a transcription factor and elucidates the regulatory mechanism for its localization.
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