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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 | 1999/06 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Heat-inactivated proteins are rescued by the DnaK center dot J-GrpE set and ClpB chaperones |
| 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 | 96(13),pp.7184-7189 |
| 著者・共著者 | K Motohashi,Y Watanabe,M Yohda,M Yoshida |
| 概要 | Functional chaperone cooperation between Hsp70 (DnaK) and Hsp104 (ClpB) was demonstrated in, vitro. In a eubacterium Thermus thermophilus. DnaK and DnaJ exist as a stable trigonal ring complex (TDnaK.J complex) and the dnaK gene cluster contains a clpB gene. When substrate proteins were heated at high temperature, none of the chaperones protected them from heat inactivation, but the TDnaK.J complex could suppress the aggregation of proteins in an ATP- and TGrpE-dependent manner. Subsequent incubation of these heated preparations at moderate temperature after addition of TClpB resulted in the efficient reactivation of the proteins. Reactivation,vas also observed, el en though the yield was low, if the substrate protein alone was heated and incubated at moderate temperature with the TDnaK.J complex, TGrpE, TClpB, and ATP. Thus, all these components were necessary for the reactivation, Further, we found that TGroEL/ES could not substitute TClpB. |
| DOI | 10.1073/pnas.96.13.7184 |
| ISSN | 0027-8424 |
| NAID | 80011200568 |
| PMID | 10377389 |