Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD.
Science
; 304(5670): 596-600, 2004 Apr 23.
Article
em En
| MEDLINE
| ID: mdl-15105503
ABSTRACT
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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Coleções:
01-internacional
Temas:
Geral
Base de dados:
MEDLINE
Assunto principal:
Peroxidases
/
Proteínas Nucleares
/
Proteínas de Choque Térmico
Limite:
Humans
Idioma:
En
Revista:
Science
Ano de publicação:
2004
Tipo de documento:
Article
País de afiliação:
Estados Unidos