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Role of the Helical Protrusion in the Conformational Change and Molecular Chaperone Activity of the Archaeal Group II Chaperonin
https://ir.soken.ac.jp/records/4320
https://ir.soken.ac.jp/records/43205b38f62e-5541-4cfb-858d-37dd45560887
| Item type | 学術雑誌論文 / Journal Article(1) | |||||||||||
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| 公開日 | 2014-03-20 | |||||||||||
| タイトル | ||||||||||||
| タイトル | Role of the Helical Protrusion in the Conformational Change and Molecular Chaperone Activity of the Archaeal Group II Chaperonin | |||||||||||
| タイトル | ||||||||||||
| タイトル | Role of the Helical Protrusion in the Conformational Change and Molecular Chaperone Activity of the Archaeal Group II Chaperonin | |||||||||||
| 言語 | en | |||||||||||
| 言語 | ||||||||||||
| 言語 | eng | |||||||||||
| 資源タイプ | ||||||||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||||||||
| 資源タイプ | journal article | |||||||||||
| アクセス権 | ||||||||||||
| アクセス権 | metadata only access | |||||||||||
| アクセス権URI | http://purl.org/coar/access_right/c_14cb | |||||||||||
| 著者 |
IIZUKA, Ryo
× IIZUKA, Ryo
× KUWAJIMA, Kunihiro
× et, al.
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| 著者別名 |
桑島, 邦博
× 桑島, 邦博
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| 抄録 | ||||||||||||
| 内容記述タイプ | Abstract | |||||||||||
| 内容記述 | To elucidate the exact role of the helical protrusion of a group II chaperonin in its molecular chaperone function, three deletion mutants of the chaperonin from a hyperthermophilic archaeum (Thermococcus sp. strain KS-1) lacking one-third, two-thirds, and the whole of the helical protrusion were constructed. The helical protrusion is thought to be substituted for the co-chaperonin GroES of a group I chaperonin and to be important for binding to unfolded proteins. Protease sensitivity assays and small angle x-ray scattering experiments were performed to demonstrate the conformation change of the wild type protein and the deletion mutants by adenine nucleotides. Whereas the binding of ATP to the wild type protein induced a structural transition corresponding to the closure of the built-in lid, it did not cause significant structural changes in deletion mutants. Although the mutants effectively protected proteins from thermal aggregation, ATP-dependent protein folding ability was remarkably diminished. We conclude that the helical protrusion is not necessarily important for binding to unfolded proteins, but its ATP-dependent conformational change mediates folding of captured unfolded proteins. | |||||||||||
| 書誌情報 |
Journal of Biological Chemistry en : Journal of Biological Chemistry 巻 279, 号 18, p. 18834-18839, 発行日 2004-02-20 |
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| 出版者 | ||||||||||||
| 出版者 | American Society for Biochemistry and Molecular Biology | |||||||||||
| ISSN | ||||||||||||
| 収録物識別子タイプ | ISSN | |||||||||||
| 収録物識別子 | 0021-9258 | |||||||||||
| DOI | ||||||||||||
| 識別子タイプ | DOI | |||||||||||
| 関連識別子 | http://doi.org/10.1074/jbc.M400839200 | |||||||||||
| 関連名称 | 10.1074/jbc.M400839200 | |||||||||||
| 権利 | ||||||||||||
| 権利情報 | © 2014 by American Society for Biochemistry and Molecular Biology | |||||||||||
