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; Seongman Kang; Sayeon Cho; Sang Chul Lee; Byoung Chul Park; Sung Goo Park

doi:10.1007/s10059-011-0029-3

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, Seongman Kang, Sayeon Cho, Sang Chul Lee, Byoung Chul Park, Sung Goo Park

Department of Life Sciences

Research output: Contribution to journal › Article › peer-review

12 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 language	English
Pages (from-to)	255-259
Number of pages	5
Journal	Molecules and cells
Volume	31
Issue number	3
DOIs	https://doi.org/10.1007/s10059-011-0029-3
Publication status	Published - 2011 Mar

Bibliographical note

Funding 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).

Keywords

Apoptosis
GAPDH
Glutathione peroxidase 3
NO stress
Nitosylation

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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10.1007/s10059-011-0029-3

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

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.",

keywords = "Apoptosis, GAPDH, Glutathione peroxidase 3, NO stress, Nitosylation",

author = "Lee, {Phil Young} and Bae, {Kwang Hee} and Jeong, {Dae Gwin} and Chi, {Seung Wook} and Moon, {Jeong Hee} and Seongman Kang and Sayeon Cho and Lee, {Sang Chul} and Park, {Byoung Chul} and Park, {Sung Goo}",

note = "Funding 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).",

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T1 - The S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase 2 is reduced by interaction with glutathione peroxidase 3 in saccharomyces cerevisiae

AU - Lee, Phil Young

AU - Bae, Kwang Hee

AU - Jeong, Dae Gwin

AU - Chi, Seung Wook

AU - Moon, Jeong Hee

AU - Kang, Seongman

AU - Cho, Sayeon

AU - Lee, Sang Chul

AU - Park, Byoung Chul

AU - Park, Sung Goo

N1 - Funding 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).

PY - 2011/3

Y1 - 2011/3

N2 - 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.

AB - 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.

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ER -

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

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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