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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 | 2001/09 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Comprehensive survey of proteins targeted by chloroplast thioredoxin |
| 執筆形態 | その他 |
| 掲載誌名 | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA |
| 出版社・発行元 | NATL ACAD SCIENCES |
| 巻・号・頁 | 98(20),pp.11224-11229 |
| 著者・共著者 | K Motohashi,A Kondoh,MT Stumpp,T Hisabori |
| 概要 | Possible target proteins of chloroplast thioredoxin (Trx) have been investigated in the stroma lysate of spinach chloroplasts. For that purpose, we immobilized a mutant of m-type Trx in which an internal cysteine at the active site was substituted with serine, on cyanogen bromide-activated resin. By using this resin, the target proteins in chloroplast were efficiently acquired when they formed the mixed-disulfide intermediates with the immobilized Trxs. We could acquire Rubisco activase (45 kDa) and 2-Cys-type peroxiredoxin (Prx), which were recently identified as targets of chloroplast Trxs. Glyceraldehyde-3-phosphate dehydrogenase and sedoheputulose 1,7-bisphosphatase, well-known thiol enzymes in the Calvin cycle, also were recognized among the collected proteins, suggesting the method is applicable for our purpose. Furthermore, four proteins were identified from a homology search of the NH2-terminal sequence of the acquired proteins: glutamine synthetase, a protein homologous to chloroplast cyclophilin, a homolog of Prx-Q, and the Rubisco small subunit. The Trx susceptibilities of the recombinant cyclophilin and Prx-Q of Arabidopsis thaliana were then examined. The method developed in the present study is thus applicable to investigate the various redox networks via Trxs and the related enzymes in the cell. |
| DOI | 10.1073/pnas.191282098 |
| ISSN | 0027-8424 |
| NAID | 80015134224 |
| PMID | 11553771 |