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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 | 2008/01 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Binary reducing equivalent pathways using NADPH-thioredoxin reductase and ferredoxin-thioredoxin reductase in the cyanobacterium Synechocystis sp Strain PCC 6803 |
| 執筆形態 | その他 |
| 掲載誌名 | PLANT AND CELL PHYSIOLOGY |
| 出版社・発行元 | OXFORD UNIV PRESS |
| 巻・号・頁 | 49(1),pp.11-18 |
| 著者・共著者 | Shoko Hishiya,Wakako Hatakeyama,Yoko Mizota,Naomi Hosoya-Matsuda,Ken Motohashi,Masahiko Ikeuchi,Toru Hisabori |
| 概要 | Thioredoxin (Trx) is a small ubiquitous protein involved in the disulfidedithiol exchange reaction occurring in cells and organelles. In vivo, Trx is reduced by Trx reductase using NADPH or photosynthetically produced reducing equivalents, and the reduced form Trx takes on the physiological functions. In the cyanobacterium Synechocystis sp. PCC6803, two Trx reductases, ferredoxin-Trx reductase (FTR) and NADPH-Trx reductase (NTR), and four typical Trx isoforms have been identified by genomic analysis. Based on analysis of the physiological features of the Trx reductase disruptants, we found that the NTRTrx pathway is important for the antioxidant system, whereas the FTRTrx pathway may play a more important role in the control of cell growth rate. In addition, by quantification of Trx abundance in the wild-type and the disruptant Synechocystis cells, we found that the gene product of slr0623, the homolog of m-type Trx in higher plants, is the most abundant Trx, and that accumulation of Trx isoforms occurs dependent on the expression of the other redox-related proteins. A study of the binary reducing equivalent pathways in cyanobacterial cells is reported here. |
| DOI | 10.1093/pcp/pcm158 |
| ISSN | 0032-0781 |
| NAID | 10027494930 |
| PMID | 18003670 |