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Chaperonin-affected refolding of α-lactalbumin: effects of nucleotides and the co-chaperonin GroES
https://ir.soken.ac.jp/records/4287
https://ir.soken.ac.jp/records/42878fbf87af-72a9-4516-967c-6720139a693f
| Item type | 学術雑誌論文 / Journal Article(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2014-03-12 | |||||
| タイトル | ||||||
| タイトル | Chaperonin-affected refolding of α-lactalbumin: effects of nucleotides and the co-chaperonin GroES | |||||
| タイトル | ||||||
| タイトル | Chaperonin-affected refolding of α-lactalbumin: effects of nucleotides and the co-chaperonin GroES | |||||
| 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 |
TADASHI, Makio
× TADASHI, Makio× ARAI, Munehito× 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 | We have studied how nucleotides (ADP, AMP-PNP, and ATP) and the co-chaperonin GroES influence the GroEL-affected refolding of apo-α-lactalbumin. The refolding reactions induced by stopped-flow pH jumps were monitored by α-lactalbumin tryptophan fluorescence. The simple single-exponential character of the free-refolding kinetics of the protein allowed us to quantitatively analyze the kinetic traces of the GroEL-affected refolding with the aid of computer simulations, and to obtain the best-fit parameters for binding between GroEL and the refolding intermediate of α-lactalbumin by the non-linear least-squares method. When GroES was absent, the interaction between GroEL and α-lactalbumin could be well represented by a “cooperative-binding” model in which GroEL has two binding sites for α-lactalbumin with the affinity of the second site being tenfold weaker than that of the first, so that there is negative cooperativity between the two sites. The affinity between GroEL and α-lactalbumin was significantly reduced when ATP was present, while ADP and AMP-PNP did not alter the affinity. A comparison of this result with those reported previously for other target proteins suggests a remarkable adjustability of the GroEL 14-mer with respect to the nucleotide-induced reduction of affinity. When GroES was present, ATP as well as ADP and AMP-PNP were effective in reducing the affinity between GroEL and the refolding intermediate of α-lactalbumin. The affinity at a saturating concentration of ADP or AMP-PNP was about ten times lower than with GroEL alone. The ADP concentration at which the acceleration of the GroEL/ES-affected refolding of αLA was observed, was higher than the concentration at which the nucleotide-induced formation of the GroEL/ES complex took place. These results indicate that GroEL/ES complex formation itself is not enough to reduce the affinity for α-lactalbumin, and that further binding of the nucleotide to the GroEL/ES complex is required to reduce the affinity. | |||||
| 書誌情報 |
Journal of Molecular Biology en : Journal of Molecular Biology 巻 293, 号 1, p. 125-137, 発行日 1999-10-15 |
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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/10.1006/jmbi.1999.3142 | |||||
| 関連名称 | 10.1006/jmbi.1999.3142 | |||||
| 権利 | ||||||
| 権利情報 | © 1999 Academic Press | |||||
