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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2011-3-28
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0219-1032
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
31
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
255-9
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pubmed:meshHeading |
pubmed-meshheading:21229323-Catalytic Domain,
pubmed-meshheading:21229323-Cell Proliferation,
pubmed-meshheading:21229323-Enzyme Assays,
pubmed-meshheading:21229323-Gene Deletion,
pubmed-meshheading:21229323-Glutathione Peroxidase,
pubmed-meshheading:21229323-Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating),
pubmed-meshheading:21229323-Nitric Oxide,
pubmed-meshheading:21229323-Oxidative Stress,
pubmed-meshheading:21229323-Protein Binding,
pubmed-meshheading:21229323-Protein Interaction Domains and Motifs,
pubmed-meshheading:21229323-Protein Processing, Post-Translational,
pubmed-meshheading:21229323-Saccharomyces cerevisiae,
pubmed-meshheading:21229323-Saccharomyces cerevisiae Proteins
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pubmed:year |
2011
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pubmed:articleTitle |
The S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase 2 is reduced by interaction with glutathione peroxidase 3 in Saccharomyces cerevisiae.
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pubmed:affiliation |
Medical Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, 305-806, Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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