The Escherichia coli btuE gene, encodes a glutathione peroxidase that is induced under oxidative stress conditions

Felipe A. Arenas, Waldo A. Díaz, Carolina A. Leal, José M. Pérez-Donoso, James A. Imlay, Claudio C. Vásquez

Research output: Contribution to journalArticlepeer-review

55 Citations (Scopus)

Abstract

Most aerobic organisms are exposed to oxidative stress. Looking for enzyme activities involved in the bacterial response to this kind of stress, we focused on the btuE-encoded Escherichia coli BtuE, an enzyme that shares homology with the glutathione peroxidase (GPX) family. This work deals with the purification and characterization of the btuE gene product.Purified BtuE decomposes in vitro hydrogen peroxide in a glutathione-dependent manner. BtuE also utilizes preferentially thioredoxin A to decompose hydrogen peroxide as well as cumene-, tert-butyl-, and linoleic acid hydroperoxides, confirming that its active site confers non-specific peroxidase activity. These data suggest that the enzyme may have one or more organic hydroperoxide as its physiological substrate.The btuE gene was induced when cells were exposed to oxidative stress elicitors that included potassium tellurite, menadione and hydrogen peroxide, among others, suggesting that BtuE could participate in the E. coli response to reactive oxygen species. To our knowledge, this is the first report describing a glutathione peroxidase in E. coli.

Original languageEnglish
Pages (from-to)690-694
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume398
Issue number4
DOIs
Publication statusPublished - Aug 2010

Keywords

  • BtuE
  • Escherichia coli
  • Oxidative stress
  • Peroxidase

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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