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タイトル: | Involvement of glutathione peroxidase 1 in growth and peroxisome formation in Saccharomyces cerevisiae in oleic acid medium. |
著者: | Ohdate, Takumi Inoue, Yoshiharu |
著者名の別形: | 井上, 善晴 |
キーワード: | Glutathione peroxidase Peroxisome Yeast Peroxiredoxin Reactive oxygen species |
発行日: | Sep-2012 |
出版者: | Elsevier B.V. |
誌名: | Biochimica et biophysica acta(BBA) - Molecular and Cell Biology of Lipids |
巻: | 1821 |
号: | 9 |
開始ページ: | 1295 |
終了ページ: | 1305 |
抄録: | Saccharomyces cerevisiae is able to use some fatty acids, such as oleic acid, as a sole source of carbon. β-oxidation, which occurs in a single membrane-enveloped organelle or peroxisome, is responsible for the assimilation of fatty acids. In S. cerevisiae, β-oxidation occurs only in peroxisomes, and H(2)O(2) is generated during this fatty acid-metabolizing pathway. S. cerevisiae has three GPX genes (GPX1, GPX2, and GPX3) encoding atypical 2-Cys peroxiredoxins. Here we show that expression of GPX1 was induced in medium containing oleic acid as a carbon source in an Msn2/Msn4-dependent manner. We found that Gpx1 was located in the peroxisomal matrix. The peroxisomal Gpx1 showed peroxidase activity using thioredoxin or glutathione as a reducing power. Peroxisome biogenesis was induced when cells were cultured with oleic acid. Peroxisome biogenesis was impaired in gpx1∆ cells, and subsequently, the growth of gpx1∆ cells was lowered in oleic acid-containing medium. Gpx1 contains six cysteine residues. Of the cysteine-substituted mutants of Gpx1, Gpx1(C36S) was not able to restore growth and peroxisome formation in oleic acid-containing medium, therefore, redox regulation of Gpx1 seems to be involved in the mechanism of peroxisome formation. |
著作権等: | © 2012 Elsevier B.V. This is not the published version. Please cite only the published version. この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。 |
URI: | http://hdl.handle.net/2433/160393 |
DOI(出版社版): | 10.1016/j.bbalip.2012.05.004 |
PubMed ID: | 22659048 |
出現コレクション: | 学術雑誌掲載論文等 |
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