| Item type |
学術雑誌論文 / Journal Article(1) |
| 公開日 |
2014-03-17 |
| タイトル |
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タイトル |
Nucleotide binding to the chaperonin GroEL: non-cooperative binding of ATP analogs and ADP, and cooperative effect of ATP |
| タイトル |
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タイトル |
Nucleotide binding to the chaperonin GroEL: non-cooperative binding of ATP analogs and ADP, and cooperative effect of ATP |
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言語 |
en |
| 言語 |
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言語 |
eng |
| 資源タイプ |
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資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
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資源タイプ |
journal article |
| アクセス権 |
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アクセス権 |
metadata only access |
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アクセス権URI |
http://purl.org/coar/access_right/c_14cb |
| 著者 |
INOBE, Tomonao
TADASHI, Makio
TAKASU-ISHIKAWA, Etsuko
TERADA, Tomoki P
KUWAJIMA, Kunihiro
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| 著者別名 |
桑島, 邦博
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| 抄録 |
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内容記述タイプ |
Abstract |
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内容記述 |
Chaperonin-assisted protein folding proceeds through cycles of ATP binding and hydrolysis by GroEL, which undergoes a large structural change by the ATP binding or hydrolysis. One of the main concerns of GroEL is the mechanism of the productive and cooperative structural change of GroEL induced by the nucleotide. We studied the cooperative nature of GroEL by nucleotide titration using isothermal titration calorimetry and fluorescence spectroscopy. Our results indicated that the binding of ADP and ATP analogs to a single ring mutant (SR1), as well as that to GroEL, was non-cooperative. Only ATP induces an apparently cooperative conformational change in both proteins. Furthermore, the fluorescence changes of pyrene-labeled GroEL indicated that GroEL has two kinds of nucleotide binding sites. The fluorescence titration result fits well with a model in which two kinds of binding sites are both non-cooperative and independent of each other. These results suggest that the binding and hydrolysis of ATP may be necessary for the cooperative transition of GroEL. |
| 書誌情報 |
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
en : Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
巻 1545,
号 1-2,
p. 160-173,
発行日 2001-02-09
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| 出版者 |
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出版者 |
Elsevier |
| ISSN |
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収録物識別子タイプ |
ISSN |
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収録物識別子 |
0006-3002 |
| DOI |
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識別子タイプ |
DOI |
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関連識別子 |
https://doi.org/10.1016/S0167-4838(00)00274-0 |
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関連名称 |
10.1016/S0167-4838(00)00274-0 |
| 権利 |
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権利情報 |
Elsevier |
