Sci. STKE, 27 April 2004
REDOX REGULATION Peroxide Signaling and Antioxidant Defense
Cells have robust antioxidant defense systems to protect them against reactive oxygen and nitrogen species. However, in eukaryotes, hydrogen peroxide is also a signaling molecule, and the enzymes that reduce peroxides, the peroxiredoxins (Prxs), can be inactivated by overoxidation of the catalytic center to allow signaling. Budanov et al. show that the sestrins, a family of proteins whose expression is modulated by p53, are required for regeneration of active Prxs. Sestrins contain a predicted redox active domain that is homologous to AhpD, the enzyme that catalyzes reduction of bacterial Prx. However, whereas AhpD is a disulfide reductase, sestrins are cysteine sulfinyl reductases.
A. V. Budanov, A. A. Sablina, E. Feinstein, E. V. Koonin, P. M. Chumakov, Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD. Science 304, 596-600 (2004). [Abstract] [Full Text]
Citation: Peroxide Signaling and Antioxidant Defense. Sci. STKE 2004, tw153 (2004).
Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882