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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 | 2002/02 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Roles of the two ATP binding sites of ClpB from Thermus thermophilus |
| 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 | 277(8),pp.5804-5809 |
| 著者・共著者 | YH Watanabe,K Motohashi,M Yoshida |
| 概要 | As a member of molecular chaperone Hsp100/Clp family, TCIpB from Thermus thermophilus has two nucleotide binding domains, NBD1 and NBD2, in a single polypeptide, each containing WalkerA and WalkerB consensus motifs. To probe their roles, mutations were introduced into the WalkerA or WalkerB motifs of each or both of the NBDs. The results are as follows. 1) For each of the NBDs, the ability of nucleotide binding is lost by mutations in the WalkerA motif but is retained by mutations in the WalkerB motif. 2) Each NBD has a casein-stimulatable small basic ATPase activity that is lost when the WalkerB motif is mutated. 3) TClpB assembles into a uniform 580-kDa oligomer when ATP is present at 55 degreesC, and only the mutants in the WalkerA motif in NBD1 fail to assemble, indicating that ATP binding to NBD1 but not hydrolysis is necessary and sufficient for the assembly. 4) Chaperone function of TClpB was lost when the WalkerA motif in each of the NBDs was mutated. Mutants in the WalkerB motifs of each NBD retained some chaperone activity. |
| DOI | 10.1074/jbc.M109349200 |
| ISSN | 0021-9258 |
| NAID | 80015173866 |
| PMID | 11741950 |