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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 | 1999/11 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | epsilon Subunit, an endogenous inhibitor of bacterial F-1-ATPase, also inhibits F0F1-ATPase |
| 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 | 274(48),pp.33991-33994 |
| 著者・共著者 | Y Kato-Yamada,D Bald,M Koike,K Motohashi,T Hisabori,M Yoshida |
| 概要 | Since the report by Sternweis and Smith (Sternweis, P. C., and Smith, J. B. (1980) Biochemistry 19, 526-531), the epsilon subunit, an endogenous inhibitor of bacterial F-1-ATPase, has long been thought not to inhibit activity of the holo enzyme, F0F1-ATPase. However, we report here that the epsilon subunit is exerting inhibition in F0F1-ATPase. We prepared a C-terminal half-truncated epsilon subunit (epsilon(Delta C)) of the thermophilic Bacillus PS3 F0F1-ATPase and reconstituted F-1- and F0F1-ATPase containing epsilon(Delta C). Compared with F-1- and F0F1-ATPase containing intact epsilon, those containing epsilon(Delta C) showed uninhibited activity; severalfold higher rate of ATP hydrolysis at low ATP concentration and the start of ATP hydrolysis without an initial lag at high ATP concentration. The F0F1-ATPase containing epsilon(Delta C) was capable of ATP-driven H+ pumping. The time-course of pumping at low ATP concentration was faster than that by the F0F1-ATPase containing intact epsilon. Thus, the comparison with noninhibitory epsilon(Delta C) mutant shed light on the inhibitory role of the intact epsilon subunit in F0F1-ATPase. |
| DOI | 10.1074/jbc.274.48.33991 |
| ISSN | 0021-9258 |
| NAID | 80010779276 |
| PMID | 10567363 |