articleScienceApr 22, 2004Closed access

Regeneration of Peroxiredoxins by p53-Regulated Sestrins, Homologs of Bacterial AhpD

Engelhardt Institute of Molecular Biology · National Institutes of Health · +4 more institutions

PubMed
Indexed incrossrefpubmed

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…

Citation impact

724
total citations
FWCI
15.07
Percentile
100%
References
29
Citations per year

Authors

5

Topics & keywords

Keywords
  • Hydrogen peroxide
  • Cysteine
  • Antioxidant
  • Biochemistry
  • Chemistry
  • Enzyme
  • Cell biology
  • Protein superfamily
No related works found for this paper.