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

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/4287
8fbf87af-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
言語 en
タイトル Chaperonin-affected refolding of α-lactalbumin: effects of nucleotides and the co-chaperonin GroES
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

WEKO 2495

TADASHI, Makio

Search repository
ARAI, Munehito

× ARAI, Munehito

WEKO 2491

ARAI, Munehito

Search repository
KUWAJIMA, Kunihiro

× KUWAJIMA, Kunihiro

WEKO 2361

KUWAJIMA, Kunihiro

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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 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
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
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