Facilitated release of substrate protein from prefoldin by chaperonin
Facilitated release of substrate protein from prefoldin by chaperonin
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DOI：
10.1016/j.febslet.2005.05.061
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发表时间：
2005-07-04
期刊：
影响因子：
3.5
通讯作者：
Funatsu, T
中科院分区：
文献类型：
--
作者：
Zako, T;Iizuka, R;Funatsu, T
前折叠蛋白是捕获蛋白质折叠中间体并将其转移到第11组伴侣蛋白以进行正确折叠的伴侣蛋白。然而，尚未研究前折叠蛋白和底物蛋白之间的相互作用的动力学。本研究首次利用荧光显微镜测定了未折叠蛋白与前折叠蛋白的解离常数和解离速率常数。我们的研究结果表明，超嗜热古菌的前折叠蛋白与底物蛋白的结合和释放处于动态平衡。有趣的是，当伴侣蛋白存在时，促进了底物蛋白从前折叠蛋白的释放，支持底物蛋白从前折叠蛋白到伴侣蛋白的传递机制。(c)2005年欧洲生物化学学会联合会。Elsevier B.V.出版，保留所有权利。
Prefoldin is a chaperone that captures a protein-folding intermediate and transfers it to the group 11 chaperonin for correct folding. However, kinetics of interactions between prefoldin and substrate proteins have not been investigated. In this study, dissociation constants and dissociation rate constants of unfolded proteins with prefoldin were firstly measured using fluorescence microscopy. Our results suggest that binding and release of prefoldin from hyperthermophilic archaea with substrate proteins were in a dynamic equilibrium. Interestingly, the release of substrate proteins from prefoldin was facilitated when chaperonin was present, supporting a handoff mechanism of substrate proteins from prefoldin to the chaperonin. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.