Glutathione peroxidase 3 of Saccharomyces cerevisiae regulates the activity of methionine sulfoxide reductase in a redox state-dependent way

Chang Won Kho, Phil Young Lee, Kwang Hee Bae, Sayeon Cho, Zee Won Lee, Byoung Chul Park, Seong Man Kang, Do Hee Lee, Sung Goo Park

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31 Citations (Scopus)


Glutathione peroxidase (Gpx) is one of the most important anti-oxidant enzymes in yeast. Gpx3 is a ubiquitously expressed isoform that modulates the activities of redox-sensitive thiol proteins, particularly those involved in signal transduction pathways and protein translocation. In order to search for the interaction partners of Gpx3, we carried out immunoprecipitation/2-dimensional gel electrophoresis (IP-2DE), MALDI-TOF mass spectrometry, and a pull down assay. We found that Mxr1, a peptide methionine sulfoxide reductase, interacts with Gpx3. By reducing methionine sulfoxide to methionine, Mxr1 reverses the inactivation of proteins caused by the oxidation of critical methionine residues. Gpx3 can interact with Mxr1 through the formation of an intermolecular disulfide bond. When oxidative stress is induced by H2O2, this interaction is compromised and the free Mxr1 then repairs the oxidized proteins. Our findings imply that this interaction links redox sensing machinery of Gpx3 to protein repair activity of Mxr1. Based on these results, we propose that Gpx3 functions as a redox-dependent exquisite regulator of the protein repair activity of Mxr1.

Original languageEnglish
Pages (from-to)25-35
Number of pages11
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - 2006 Sep 15



  • Disulfide bond
  • Gpx3
  • Mxr1
  • Oxidative stress
  • ROS

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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