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首页> 外文期刊>Journal of Molecular Biology >Chaperonin GroEL-GroES Functions as both Alternating and Non-Alternating Engines
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Chaperonin GroEL-GroES Functions as both Alternating and Non-Alternating Engines

机译：伴侣蛋白GroEL-GroES既可作为交替发动机又可作为非交替发动机

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A double ring-shaped GroEL consisting of 14 ATPase subunits assists protein folding, together with co-chaperonin GroES. The dynamic GroEL-GroES interaction is actively involved in the chaperonin reaction. Therefore, revealing this dynamic interaction is a key to understanding the operation principle of GroEL. Nevertheless, how this interaction proceeds in the reaction cycle has long been controversial. Here, we directly imaged GroEL-GroES interaction in the presence of disulfide-reduced a-lactalbumin as a substrate protein using high-speed atomic force microscopy. This real-time imaging revealed the occurrence of primary, symmetric GroEL:GroES(2) and secondary, asymmetric GroEL:GroES(1) complexes. Remarkably, the reaction was observed to often branch into main and side pathways. In the main pathway, alternate binding and release of GroES occurs at the two rings, indicating tight cooperation between the two rings. In the side pathway, however, this cooperation is disrupted, resulting in the interruption of alternating rhythm. From various properties observed for both pathways, we provide mechanistic insight into the alternate and non-alternate operations of the two-engine system. (C) 2016 Elsevier Ltd. All rights reserved.
机译：由14个ATPase亚基组成的双环形GroEL与伴侣蛋白GroES一起辅助蛋白质折叠。动态GroEL-GroES相互作用积极参与伴侣蛋白反应。因此，揭示这种动态相互作用是理解GroEL操作原理的关键。然而，这种相互作用如何在反应周期中进行一直是有争议的。在这里，我们使用高速原子力显微镜在存在二硫化物还原的α-乳白蛋白作为底物蛋白的情况下直接成像了GroEL-GroES相互作用。该实时成像显示了主要的对称GroEL：GroES（2）和次要的非对称GroEL：GroES（1）复合物的出现。值得注意的是，观察到该反应经常分支为主要途径和副途径。在主要途径中，GroES的交替结合和释放发生在两个环上，表明两个环之间紧密协作。然而，在旁路中，这种合作被破坏，导致交替节奏的中断。从对两种途径观察到的各种特性，我们提供了对双引擎系统的交替和非交替操作的机械洞察力。 （C）2016 Elsevier Ltd.保留所有权利。

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