| pubmed-article:16401067 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16401067 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:16401067 | lifeskim:mentions | umls-concept:C0537086 | lld:lifeskim |
| pubmed-article:16401067 | lifeskim:mentions | umls-concept:C0633227 | lld:lifeskim |
| pubmed-article:16401067 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:16401067 | lifeskim:mentions | umls-concept:C0439851 | lld:lifeskim |
| pubmed-article:16401067 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:16401067 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:16401067 | lifeskim:mentions | umls-concept:C1552596 | lld:lifeskim |
| pubmed-article:16401067 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:16401067 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:16401067 | lifeskim:mentions | umls-concept:C1947931 | lld:lifeskim |
| pubmed-article:16401067 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:16401067 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:16401067 | pubmed:dateCreated | 2006-1-10 | lld:pubmed |
| pubmed-article:16401067 | pubmed:abstractText | Glutathione S-transferase pi (GST pi) has been shown to reactivate oxidized 1-cysteine peroxiredoxin (1-Cys Prx, Prx VI, Prdx6, and AOP2). We now demonstrate that a heterodimer complex is formed between 1-Cys Prx with a C-terminal His6 tag and GST pi upon incubation of the two proteins at pH 8.0 in buffer containing 20% 1,6-hexanediol to dissociate the homodimers, followed by dialysis against buffer containing 2.5 mM glutathione (GSH) but lacking 1,6-hexanediol. The heterodimer can be purified by chromatography on nickel-nitriloacetic acid agarose in the presence of GSH. N-Terminal sequencing showed that equimolar amounts of the two proteins are present in the isolated complex. In the heterodimer, 1-Cys Prx is fully active toward either H2O2 or phospholipid hydroperoxide, while the GST pi activity is approximately 25% of that of the GST pi homodimer. In contrast, the 1-Cys Prx homodimer lacks peroxidase activity even in the presence of free GSH. The heterodimer is also formed in the presence of S-methylglutathione, but no 1-Cys Prx activity is found under these conditions. The yield of heterodimer is decreased in the absence of 1,6-hexanediol or GSH. Rapid glutathionylation of 1-Cys Prx in the heterodimer is detected by immunoblotting. Subsequently, a disulfide-linked dimer is observed on SDS-PAGE, and the free cysteine content is decreased by 2 per heterodimer. The involvement of particular binding sites in heterodimer formation was tested by site-directed mutagenesis of the two proteins. For 1-Cys Prx, neither Cys47 nor Ser32 is required for heterodimer formation but Cys47 is essential for 1-Cys Prx activation. For GST pi, Cys47 and Tyr7 (at or near the GSH-binding site) are needed for heterodimer formation but three other cysteines are not. We conclude that reactivation of oxidized 1-Cys Prx by GST pi occurs by heterodimerization of 1-Cys Prx and GST pi harboring bound GSH, followed by glutathionylation of 1-Cys Prx and then formation of an intersubunit disulfide. Finally, the GSH-mediated reduction of the disulfide regenerates the reduced active-site sulfhydryl of 1-Cys Prx. | lld:pubmed |
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| pubmed-article:16401067 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:16401067 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16401067 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16401067 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:16401067 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:16401067 | pubmed:author | pubmed-author:FisherAron... | lld:pubmed |
| pubmed-article:16401067 | pubmed:author | pubmed-author:ColmanRoberta... | lld:pubmed |
| pubmed-article:16401067 | pubmed:author | pubmed-author:ManevichYefim... | lld:pubmed |
| pubmed-article:16401067 | pubmed:author | pubmed-author:RalatLuis ALA | lld:pubmed |
| pubmed-article:16401067 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16401067 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:16401067 | pubmed:volume | 45 | lld:pubmed |
| pubmed-article:16401067 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16401067 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16401067 | pubmed:pagination | 360-72 | lld:pubmed |
| pubmed-article:16401067 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:16401067 | pubmed:meshHeading | pubmed-meshheading:16401067... | lld:pubmed |
| pubmed-article:16401067 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16401067 | pubmed:articleTitle | Direct evidence for the formation of a complex between 1-cysteine peroxiredoxin and glutathione S-transferase pi with activity changes in both enzymes. | lld:pubmed |
| pubmed-article:16401067 | pubmed:affiliation | Department of Chemistry and Biochemistry, University of Delaware, Newark, Delaware 19716, USA. | lld:pubmed |
| pubmed-article:16401067 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16401067 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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