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Mol. Cells 2011; 31(3): 255-259

Published online December 30, 2011

https://doi.org/10.1007/s10059-011-0029-3

© The Korean Society for Molecular and Cellular Biology

The S-Nitrosylation of Glyceraldehyde-3-Phosphate Dehydrogenase 2 Is Reduced by Interaction with Glutathione Peroxidase 3 in Saccharomyces cerevisiae

Phil Young Lee1,2,4, Kwang-Hee Bae1,4, Dae Gwin Jeong1, Seung-Wook Chi1, Jeong Hee Moon1, Seongman Kang2, Sayeon Cho3, Sang Chul Lee1, Byoung Chul Park1,*, and Sung Goo Park1,*

1Medical Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-806, Korea, 2School of Biotechnology, Korea University, Seoul 136-701, Korea, 3College of Pharmacy, Chung-Ang University, Seoul 156-756, Korea, 4These authors contributed equally to this work.

Correspondence to : *Correspondence: sgpark@kribb.re.kr (SGP); parkbc@kribb.re.kr (BCP)

Received: September 13, 2010; Revised: November 26, 2010; Accepted: December 10, 2010

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 biologi-cal 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.

Keywords Apoptosis, GAPDH, glutathione peroxidase 3, nitosylation, NO stress

Article

Research Article

Mol. Cells 2011; 31(3): 255-259

Published online March 31, 2011 https://doi.org/10.1007/s10059-011-0029-3

Copyright © The Korean Society for Molecular and Cellular Biology.

The S-Nitrosylation of Glyceraldehyde-3-Phosphate Dehydrogenase 2 Is Reduced by Interaction with Glutathione Peroxidase 3 in Saccharomyces cerevisiae

Phil Young Lee1,2,4, Kwang-Hee Bae1,4, Dae Gwin Jeong1, Seung-Wook Chi1, Jeong Hee Moon1, Seongman Kang2, Sayeon Cho3, Sang Chul Lee1, Byoung Chul Park1,*, and Sung Goo Park1,*

1Medical Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-806, Korea, 2School of Biotechnology, Korea University, Seoul 136-701, Korea, 3College of Pharmacy, Chung-Ang University, Seoul 156-756, Korea, 4These authors contributed equally to this work.

Correspondence to:*Correspondence: sgpark@kribb.re.kr (SGP); parkbc@kribb.re.kr (BCP)

Received: September 13, 2010; Revised: November 26, 2010; Accepted: December 10, 2010

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 biologi-cal 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.

Keywords: Apoptosis, GAPDH, glutathione peroxidase 3, nitosylation, NO stress

Mol. Cells
Jun 30, 2023 Vol.46 No.6, pp. 329~398
COVER PICTURE
The cellular proteostasis network is adaptively modulated upon cellular stress, thereby protecting cells from proteostasis collapse. Heat shock induces the translocation of misfolded proteins and the chaperone protein HSP70 into nucleolus, where nuclear protein quality control primarily occurs. Nuclear RNA export factor 1 (green), nucleolar protein fibrillarin (red), and nuclei (blue) were visualized in NIH3T3 cells under basal (left) and heat shock (right) conditions (Park et al., pp. 374-386).

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