Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD.

Authors:
Budanov AV, Sablina AA, Feinstein E, Koonin EV, Chumakov PM
Associated Labs:
Sablina Lab (Katholieke Universiteit Leuven)
Science. 2004 Apr 23. 304(5670):596-600.
PMID: 15105503
Acting as a signal, hydrogen peroxide circumvents antioxidant defense by overoxidizing peroxiredoxins (Prxs), the enzymes that metabolize peroxides. We show that sestrins, a family of proteins whose expression is modulated by p53, are required for regeneration of Prxs containing Cys-SO(2)H, thus reestablishing the antioxidant firewall. Sestrins contain a predicted redox-active domain homologous to AhpD, the enzyme catalyzing the reduction of a bacterial Prx, AhpC. Purified Hi95 (sestrin 2) protein supports adenosine triphosphate-dependent reduction of overoxidized PrxI in vitro, indicating that unlike AhpD, which is a disulfide reductase, sestrins are cysteine sulfinyl reductases. As modulators of peroxide signaling and antioxidant defense, sestrins constitute potential therapeutic targets.

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