Glutathione peroxidases (Gpxs) are the key anti-oxidant enzymes found in Saccharomyces cerevisiae. Among the three Gpx isoforms, glutathione peroxidase 3 (Gpx3) is ubiquitously expressed and modulates the activities of redox-sensitive thiol proteins involved in various biological reactions. By using a proteomic approach, glyceralde-hyde-3-phosphate dehydrogenase 2 (GAPDH2; EC 18.104.22.168) was found as a candidate protein for interaction with Gpx3. GAPDH, a key enzyme in glycolysis, is a multi-functional protein with multiple intracellular localizations and diverse activities. To validate the interaction between Gpx3 and GAPDH2, immunoprecipitation and a pull-down assay were carried out. The results clearly showed that GAPDH2 interacts with Gpx3 through its carboxyl-terminal domain both in vitro and in vivo. Additionally, Gpx3 helps to reduce the S-nitrosylation of GAPDH upon nitric oxide (NO) stress; this subsequently increases cellular viability. On the basis of our findings, we suggest that Gpx3 protects GAPDH from NO stress and thereby contributes to the maintenance of homeostasis during exposure to NO stress.
Bibliographical noteFunding Information:
We thank Dr. Eui-Jeon Woo for helpful advices and Dr. Sunghyun Kang for critical reading of the manuscript. This research was supported by grants from Korea Research Institute of Bioscience and Biotechnology Open Innovation Program (to K.-H. Bae), National Research Foundation of Korea (to S.G. Park, Grant No. 2010-0008754 ), Mid-career Research Program (to K.-H. Bae, Grant No. 2010-0022319) and Happy Technology Program through the National Research Foundation of Korea (to B.C. Park, Grant No. 2010-0020765).
- Glutathione peroxidase 3
- NO stress
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology