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Specificity in chaperonin-mediated protein folding.

机译：伴侣蛋白介导的蛋白质折叠的特异性。

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摘要

Chaperonins are ubiquitous multisubunit toroidal complexes that aid protein folding in an ATP-dependent manner. Current models of folding by the bacterial chaperonin GroEL depict its role as unfolding and releasing molecules that have misfolded, so that they can return to a potentially productive folding pathway in solution. Accordingly, a given target polypeptide might require several cycles of binding and ATP-driven release from different chaperonin complexes before reaching the native state. Surprisingly, cycling of a target protein does not guarantee its folding, and we report here that unfolded beta-actin or alpha-tubulin both form tight complexes when presented to either GroEL or its mitochondrial homologue, and both undergo cycles of release and rebinding upon incubation with ATP, but no native protein is produced. We conclude that different chaperonins produce distinctive spectra of folding intermediates.
机译：伴侣蛋白是无处不在的多亚基环状复合物，以ATP依赖性方式帮助蛋白质折叠。当前细菌伴侣蛋白GroEL的折叠模型描述了其作为展开和释放已错误折叠的分子的作用，因此它们可以返回到溶液中可能具有生产力的折叠路径。因此，给定的靶多肽在到达天然状态之前可能需要几个结合和ATP驱动的释放从不同的伴侣蛋白复合物中的循环。出乎意料的是，靶蛋白的循环不能保证其折叠，我们在此报告，未折叠的β-肌动蛋白或α-微管蛋白在呈递给GroEL或其线粒体同源物时均形成紧密的复合物，并且均经过释放和保温后的结合循环ATP，但不会产生天然蛋白质。我们得出结论，不同的伴侣蛋白产生独特的折叠中间体谱。

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