Molecules and Cells

, Volume 31, Issue 3, pp 255–259

The S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase 2 is reduced by interaction with glutathione peroxidase 3 in Saccharomyces cerevisiae

Authors

  • Phil Young Lee
    • Medical Proteomics Research CenterKorea Research Institute of Bioscience and Biotechnology
    • School of BiotechnologyKorea University
  • Kwang-Hee Bae
    • Medical Proteomics Research CenterKorea Research Institute of Bioscience and Biotechnology
  • Dae Gwin Jeong
    • Medical Proteomics Research CenterKorea Research Institute of Bioscience and Biotechnology
  • Seung-Wook Chi
    • Medical Proteomics Research CenterKorea Research Institute of Bioscience and Biotechnology
  • Jeong Hee Moon
    • Medical Proteomics Research CenterKorea Research Institute of Bioscience and Biotechnology
  • Seongman Kang
    • School of BiotechnologyKorea University
  • Sayeon Cho
    • College of PharmacyChung-Ang University
  • Sang Chul Lee
    • Medical Proteomics Research CenterKorea Research Institute of Bioscience and Biotechnology
    • Medical Proteomics Research CenterKorea Research Institute of Bioscience and Biotechnology
    • Medical Proteomics Research CenterKorea Research Institute of Bioscience and Biotechnology
Article

DOI: 10.1007/s10059-011-0029-3

Cite this article as:
Lee, P.Y., Bae, K., Jeong, D.G. et al. Mol Cells (2011) 31: 255. doi:10.1007/s10059-011-0029-3

Abstract

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, glyceraldehyde-3-phosphate dehydrogenase 2 (GAPDH2; EC 1.2.1.12) 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.

Keywords

ApoptosisGAPDHglutathione peroxidase 3NitosylationNO stress

Copyright information

© The Korean Society for Molecular and Cellular Biology and Springer Netherlands 2011