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モトハシ タケシ
MOTOHASHI TAKESHI
本橋 健 所属 京都産業大学 生命科学部 先端生命科学科 職種 教授 |
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| 言語種別 | 英語 |
| 発行・発表の年月 | 2003/08 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Chloroplast cyclophilin is a target protein of thioredoxin - Thiol modulation of the peptidyl-prolyl cis-trans isomerase activity |
| 執筆形態 | その他 |
| 掲載誌名 | JOURNAL OF BIOLOGICAL CHEMISTRY |
| 出版社・発行元 | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
| 巻・号・頁 | 278(34),pp.31848-31852 |
| 著者・共著者 | K Motohashi,F Koyama,Y Nakanishi,H Ueoka-Nakanishi,T Hisabori |
| 概要 | Chloroplast cyclophilin has been identified as a potential candidate of enzymes in chloroplasts that are regulated by thioredoxin ( Motohashi, K., Kondoh, A., Stumpp, M. T., and Hisabori, T. ( 2001) Proc. Natl. Acad. Sci. U. S. A. 98, 11224 - 11229). In the present study we found that the peptidyl-prolyl cis-trans isomerase activity of cyclophilin is fully inactivated in the oxidized form. Reduction of cyclophilin by thioredoxin-m recovered the isomerase activity. Two crucial disulfide bonds were determined by disulfide-linked peptide mapping. The relevance of these cysteines for isomerase activity was confirmed by the mutagenesis studies. Because four cysteine residues in Arabidopsis thaliana cyclophilin were conserved in the isoforms from several organisms, it appears that this redox regulation must be one of the common regulation systems of cyclophilin. |
| DOI | 10.1074/jbc.M304258200 |
| ISSN | 0021-9258 |
| NAID | 80016138545 |
| PMID | 12923164 |