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Φ Value Analysis of an Allosteric Transition of GroEL based on a Single-pathway Model
https://ir.soken.ac.jp/records/4318
https://ir.soken.ac.jp/records/4318559500e2-b26a-4d3b-90e4-ae79113bedbc
| 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 | Φ Value Analysis of an Allosteric Transition of GroEL based on a Single-pathway Model | |||||
| タイトル | ||||||
| タイトル | Φ Value Analysis of an Allosteric Transition of GroEL based on a Single-pathway Model | |||||
| 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 |
INOBE, Tomonao
× INOBE, Tomonao× KUWAJIMA, Kunihiro |
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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 | There are currently two contradictory models for the kinetics of the ATP-induced GroEL allosteric transition occurring around 20 μM ATP. One model, proposed by Horovitz et al. demonstrates the existence of two parallel pathways for the allosteric transition and an abrupt ATP-dependent switch from one pathway to the other. The other model, which was proposed by the present authors, shows no need to assume the parallel pathways, and a combination of the transition-state theory and the Monod–Wyman–Changeux model of allostery can explain the kinetics as well as the equilibrium of the transition. The discrepancy appears to be due to whether we regard the transition as reversible or irreversible. Thus, here we have investigated the reversibility of the allosteric transition between 0 μM and 70 μM ATP by the use of a stopped-flow double-jump technique, which has allowed us to monitor the kinetics of the reverse reaction from the relaxed state at a high ATP concentration to the tense state at a low ATP concentration. The tryptophan fluorescence of a tryptophan-inserted variant of GroEL was used to follow the kinetics. As a result, the allosteric transition was shown to be a reversible process, supporting the validity of our model. We also show that the structural environment around the ATP-binding site of GroEL in the transition state is very similar to that in the relaxed state (Φ=0.9) by using a Φ value analysis in the kinetic Monod–Wyman–Changeux model, which is analogous to the mutational Φ value analysis in protein folding. | |||||
| 書誌情報 |
Journal of Molecular Biology en : Journal of Molecular Biology 巻 339, 号 1, p. 199-205, 発行日 2004-05-21 |
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| 出版者 | ||||||
| 出版者 | Elsevier | |||||
| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 0022-2836 | |||||
| DOI | ||||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | https://doi.org/10.1016/j.jmb.2004.03.026 | |||||
| 関連名称 | 10.1016/j.jmb.2004.03.026 | |||||
| 権利 | ||||||
| 権利情報 | © 2004 Elsevier Ltd. | |||||
