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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 | 2000/12 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Inverse regulation of F-1-ATPase activity by a mutation at the regulatory region on the gamma subunit of chloroplast ATP synthase |
| 執筆形態 | その他 |
| 掲載誌名 | BIOCHEMICAL JOURNAL |
| 出版社・発行元 | PORTLAND PRESS LTD |
| 巻・号・頁 | 352(3),pp.783-788 |
| 著者・共著者 | H Konno,M Yodogawa,MT Stumpp,P Kroth,H Strotmann,K Motohashi,T Amano,T Hisabori |
| 概要 | Chloroplast ATP synthase is a thiol-modulated enzyme whose Delta muH(+)-linked activation is strongly influenced by reduction and the formation of a disulphide bridge between Cys(199) and Cys(205) on the gamma subunit. In solubilized chloroplast coupling factor 1 (CF1), reduction of the disulphide bond elicits the latent ATP-hydrolysing activity. To assess the regulatory importance of the amino acid residues around these cysteine residues, we focused on the three negatively charged residues Glu(210)-Asp-Glu(212) close to the two cysteine residues and also on the following region from Leu(213) to Ile(230), and investigated the rnodulation of ATPase activity by chloroplast thioredoxins. The mutant gamma subunits were reconstituted with the alpha and beta subunits from F-1 of the thermophilic bacterium Bacillus PS3; the active ATPase complexes obtained were purified by gel-filtration chromatography. The complex formed with a mutant gamma subunit in which Glu(210) to Glu(212) had been deleted was inactivated rather than activated by reduction of the disulphide bridge by reduced thioredoxin, indicating inverse regulation. This complex was insensitive to the inhibitory CF1-epsilon subunit when the mutant gamma subunit was oxidized. In contrast, the deletion of Glu(212) to Ile(230) converted the complex from a modulated state into a highly active state. |
| DOI | 10.1042/0264-6021:3520783 |
| ISSN | 0264-6021/1470-8728 |
| NAID | 80012018927 |
| PMID | 11104686 |