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

Phil Young Lee, Kwang Hee Bae, Dae Gwin Jeong, Seung Wook Chi, Jeong Hee Moon, Seong Man Kang, Sayeon Cho, Sang Chul Lee, Byoung Chul Park, Sung Goo Park

Research output: Contribution to journalArticle

11 Citations (Scopus)

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, glyceralde-hyde-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.

Original languageEnglish
Pages (from-to)255-259
Number of pages5
JournalMolecules and Cells
Volume31
Issue number3
DOIs
Publication statusPublished - 2011 Mar 1

Keywords

  • Apoptosis
  • GAPDH
  • Glutathione peroxidase 3
  • Nitosylation
  • NO stress

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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