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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 | 2000/05 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | FtsH recognizes proteins with unfolded structure and hydrolyzes the carboxyl side of hydrophobic residues |
| 執筆形態 | その他 |
| 掲載誌名 | JOURNAL OF BIOCHEMISTRY |
| 出版社・発行元 | OXFORD UNIV PRESS |
| 巻・号・頁 | 127(5),pp.931-937 |
| 著者・共著者 | Y Asahara,K Atsuta,K Motohashi,H Taguchi,M Yohda,M Yoshida |
| 概要 | FtsH of Escherichia coli is an essential membrane-integrated ATP-dependent protease. We cloned a gene for an FtsH homolog (T.FtsH) from Thermus thermophilus HB8, expressed it in E. coli, and purified the expressed protein. ATPase activity of T.FtsH was activated by proteins with unfolded structure (alpha-casein and pepsin), and T.FtsH digested these proteins in an ATP-, Zn2+-dependent manner. alpha-Lactalbumin was digested by T.FtsH when it was largely unfolded, but not in its native form. Analysis of the proteolytic products revealed that, in most cases, T.FtsH cleaved the C-terminal side of hydrophobic residues and produced a characteristic set of small peptides (<30 kDa) without releasing a large intermediate. Thus, T.FtsH recognizes the unfolded structure of the proteins and progressively digests them at the expense of ATP. A soluble domain of T.FtsH, which lacked the N-terminal two transmembrane helices, was also prepared but was found to retain neither ATPase nor protease activities. Thus, the membrane segment appeared to be indispensable for these activities of T.FtsH. |
| ISSN | 0021-924X/1756-2651 |
| Put Code(ORCID) | 21490280 |
| PermalinkURL | http://www.scopus.com/inward/record.url?eid=2-s2.0-0034079766&partnerID=MN8TOARS |
| researchmap用URL | http://orcid.org/0000-0002-8414-2836 |