Identification of in vivo substrates of the chaperonin GroEL
Identification of in vivo substrates of the chaperonin GroEL
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DOI：
10.1038/45977
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发表时间：
1999-11-11
期刊：
影响因子：
64.8
通讯作者：
Hartl, FU
中科院分区：
文献类型：
--
作者：
Houry, WA;Frishman, D;Hartl, FU
伴侣蛋白GroEL在介导大肠杆菌胞浆蛋白折叠中起重要作用。在这里，我们发现GroEL与一组定义良好的大约300个新翻译的多肽有强烈的相互作用，包括转录/翻译机制和代谢酶的基本成分。这些蛋白质中约有三分之一结构不稳定，反复返回GroEL进行构象维护。GroEL底物优先由两个或多个具有ap折叠的结构域组成，其中包含a-螺旋和具有广泛疏水表面的埋藏p-片。这些蛋白质折叠缓慢，易于聚集。GroEL的疏水结合区可能很好地适应与ap结构域蛋白的非天然状态相互作用。
The chaperonin GroEL has an essential role in mediating protein folding in the cytosol of Escherichia coli. Here we show that GroEL interacts strongly with a well-defined set of approximately 300 newly translated polypeptides, including essential components of the transcription/translation machinery and metabolic enzymes. About one third of these proteins are structurally unstable and repeatedly return to GroEL for conformational maintenance. GroEL substrates consist preferentially of two or more domains with ap-folds, which contain a-helices and buried P-sheets with extensive hydrophobic surfaces. These proteins are expected to fold slowly and be prone to aggregation. The hydrophobic binding regions of GroEL may be well adapted to interact with the non-native states of ap-domain proteins.