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首页> 外文期刊>Journal of Molecular Biology >Amyloid-like fibril formation of co-chaperonin GroES: Nucleation and extension prefer different degrees of molecular compactness
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Amyloid-like fibril formation of co-chaperonin GroES: Nucleation and extension prefer different degrees of molecular compactness

机译：陪伴蛋白GroES的淀粉样样原纤维形成：成核和延伸倾向于不同程度的分子致密性

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The molecular chaperone GroES, together with GroEL from Escherichia coli, is the best characterized protein of the molecular chaperone family. Here, we report on the in vitro formation of GroES amyloid-like fibrils and the mechanism of formation. When incubated for several weeks at neutral pH in the presence of the denaturant guanidine hydrochloride, GroES formed a typical amyloid fibril; unbranched, twisted, and extended filaments stainable by thioflavin T and Congo red. GroES fibril formation was accelerated by the addition of preformed fibril seeds, in accordance with a nucleation-extension mechanism. Interestingly, whereas the spontaneous formation of GroES fibrils was favored in the structural transition region of GroES dissociation/ unfolding, the extension of fibrils from preformed fibril seeds was favored in the region corresponding to an expanded molecular state. We concluded that the two stages of GroES fibril formation prefer different molecular states of the same protein. The significance of this preference is discussed. (c) 2005 Elsevier Ltd. All rights reserved.
机译：分子伴侣GroES，与来自大肠杆菌的GroEL一起，是分子伴侣家族中最有特色的蛋白质。在这里，我们报道了GroES淀粉样样原纤维的体外形成及其形成机理。当在变性盐酸胍存在下于中性pH下孵育数周时，GroES形成了典型的淀粉样原纤维。不分支，扭曲和延伸的细丝，可被硫黄素T和刚果红染色。根据成核-延伸机理，通过添加预形成的原纤维种子来加速GroES原纤维的形成。有趣的是，虽然GroES原纤维的自发形成在GroES解离/解折叠的结构过渡区域中受到支持，但从预形成的原纤维种子中原纤维的延伸在与扩展的分子状态相对应的区域中受到促进。我们得出的结论是，GroES原纤维形成的两个阶段偏好同一蛋白质的不同分子状态。讨论了此首选项的重要性。 （c）2005 Elsevier Ltd.保留所有权利。

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