Glutathione peroxidase 3 of Saccharomyces cerevisiae suppresses non-enzymatic proteolysis of glutamine synthetase in an activity-independent manner

Phil Young Lee, Chang Won Kho, Do Hee Lee, Sunghyun Kang, Seongman Kang, Sang Chul Lee, Byoung Chul Park, Sayeon Cho, Kwang Hee Bae, Sung Goo Park

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Glutathione peroxidase 3 (Gpx3) is ubiquitously expressed and is important antioxidant enzyme in yeast. It modulates the activities of redox-sensitive thiol proteins, particularly those involved in signal transduction pathway and protein translocation. Through immunoprecipitation/two-dimensional gel electrophoresis (IP-2DE), MALDI-TOF mass spectrometry, and a pull down assay, we found glutamine synthetase (GS; EC 6.3.1.2) as a candidate interacting protein with Gpx3. GS is a key enzyme in nitrogen metabolism and ammonium assimilation. It has been known that GS is non-enzymatically cleaved by ROS generated by MFO (thiol/ Fe3+/O2 mixed-function oxidase) system. In this study, it is demonstrated that GS interacts with Gpx3 through its catalytic domain both in vivo and in vitro regardless of redox state. In addition, Gpx3 helps to protect GS from inactivation and degradation via oxidative stress in an activity-independent manner. Based on the results, it is suggested that Gpx3 protects GS from non-enzymatic proteolysis, thereby contributing to cell homeostasis when cell is exposed to oxidative stress.

Original languageEnglish
Pages (from-to)405-409
Number of pages5
JournalBiochemical and biophysical research communications
Volume362
Issue number2
DOIs
Publication statusPublished - 2007 Oct 19

Keywords

  • Glutamine synthetase
  • Glutathione peroxidase 3
  • MFO system
  • Oxidative stress
  • ROS

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Glutathione peroxidase 3 of Saccharomyces cerevisiae suppresses non-enzymatic proteolysis of glutamine synthetase in an activity-independent manner'. Together they form a unique fingerprint.

  • Cite this