How do chaperonins fold protein?
How do chaperonins fold protein?
复制标题
DOI：
10.2142/biophysics.11.93
复制
发表时间：
2015
期刊：
影响因子：
--
通讯作者：
Motojima F
中科院分区：
文献类型：
--
作者：
Motojima F
蛋白质折叠是一个生物学过程，对于所有生物体中蛋白质的正常功能至关重要。在细胞中，许多蛋白质的折叠需要分子伴侣的帮助。伴侣蛋白属于一类已被广泛研究的分子伴侣。然而，伴侣蛋白介导蛋白质折叠的机制仍然存在争议。变性蛋白在封闭的伴侣蛋白笼中折叠，导致变性蛋白完全包封在伴侣蛋白笼内的假设。相反的假设，我们最近发现，变性蛋白质相互作用的疏水残基在亚基界面的伴侣蛋白，并部分突出的笼子。在这篇综述中，我们将解释我们最近的研究结果，并介绍我们的模型的机制，伴侣蛋白加速蛋白质折叠，鉴于最近的研究结果。
Protein folding is a biological process that is essential for the proper functioning of proteins in all living organisms. In cells, many proteins require the assistance of molecular chaperones for their folding. Chaperonins belong to a class of molecular chaperones that have been extensively studied. However, the mechanism by which a chaperonin mediates the folding of proteins is still controversial. Denatured proteins are folded in the closed chaperonin cage, leading to the assumption that denatured proteins are completely encapsulated inside the chaperonin cage. In contrast to the assumption, we recently found that denatured protein interacts with hydrophobic residues at the subunit interfaces of the chaperonin, and partially protrude out of the cage. In this review, we will explain our recent results and introduce our model for the mechanism by which chaperonins accelerate protein folding, in view of recent findings.