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Characterization of Archaeal Group II Chaperonin-ADP-Metal Fluoride Complexes
https://ir.soken.ac.jp/records/4326
https://ir.soken.ac.jp/records/43263ad8af88-e2aa-4922-9791-9aff5a7eb084
| Item type | 学術雑誌論文 / Journal Article(1) | |||||||||||
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| 公開日 | 2014-03-24 | |||||||||||
| タイトル | ||||||||||||
| タイトル | Characterization of Archaeal Group II Chaperonin-ADP-Metal Fluoride Complexes | |||||||||||
| タイトル | ||||||||||||
| タイトル | Characterization of Archaeal Group II Chaperonin-ADP-Metal Fluoride Complexes | |||||||||||
| 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 | Group II chaperonins, found in Archaea and in the eukaryotic cytosol, act independently of a cofactor corresponding to GroES of group I chaperonins. Instead, the helical protrusion at the tip of the apical domain forms a built-in lid of the central cavity. Although many studies on the lid's conformation have been carried out, the conformation in each step of the ATPase cycle remains obscure. To clarify this issue, we examined the effects of ADP-aluminum fluoride (AlFx) and ADP-beryllium fluoride (BeFx) complexes on α-chaperonin from the hyperthermophilic archaeum, Thermococcus sp. strain KS-1. Biochemical assays, electron microscopic observations, and small angle x-ray scattering measurements demonstrate that α-chaperonin incubated with ADP and BeFx exists in an asymmetric conformation; one ring is open, and the other is closed. The result indicates that α-chaperonin also shares the inherent functional asymmetry of bacterial and eukaryotic cytosolic chaperonins. Most interestingly, addition of ADP and BeFx induced α-chaperonin to encapsulate unfolded proteins in the closed ring but did not trigger their folding. Moreover, α-chaperonin incubated with ATP and AlFx or BeFx adopted a symmetric closed conformation, and its functional turnover was inhibited. These forms are supposed to be intermediates during the reaction cycle of group II chaperonins. | |||||||||||
| 書誌情報 |
Journal of Biological Chemistry en : Journal of Biological Chemistry 巻 280, 号 48, p. 40375-40383, 発行日 2005-12-02 |
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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.M506785200 | |||||||||||
| 関連名称 | 10.1074/jbc.M506785200 | |||||||||||
| 権利 | ||||||||||||
| 権利情報 | © 2014 by American Society for Biochemistry and Molecular Biology | |||||||||||
