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

Authors
Lee, Phil YoungBae, Kwang-HeeJeong, Dae GwinChi, Seung-WookMoon, Jeong HeeKang, SeongmanCho, SayeonLee, Sang ChulPark, Byoung ChulPark, Sung Goo
Issue Date
3월-2011
Publisher
KOREAN SOC MOLECULAR & CELLULAR BIOLOGY
Keywords
Apoptosis; GAPDH; glutathione peroxidase 3; nitosylation; NO stress
Citation
MOLECULES AND CELLS, v.31, no.3, pp.255 - 259
Indexed
SCIE
SCOPUS
KCI
Journal Title
MOLECULES AND CELLS
Volume
31
Number
3
Start Page
255
End Page
259
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/112898
DOI
10.1007/s10059-011-0029-3
ISSN
1016-8478
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.
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