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  1. 010 学術雑誌論文
  2. 桑島, 邦博 / KUWAJIMA, Kunihiro

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/4320
5b38f62e-5541-4cfb-858d-37dd45560887
Item type 学術雑誌論文 / Journal Article(1)
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
言語 en
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
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

WEKO 2521

IIZUKA, Ryo

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KUWAJIMA, Kunihiro

× KUWAJIMA, Kunihiro

WEKO 2361

KUWAJIMA, Kunihiro

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et, al.

× et, al.

WEKO 3119

et, al.

Search repository
著者別名 桑島, 邦博

× 桑島, 邦博

WEKO 2364
NRID 1000070091444
e-Rad 70091444

桑島, 邦博

Search repository
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
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
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