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首页> 美国卫生研究院文献>PLoS Computational Biology >Intrinsically Disordered Proteins Display No Preference for Chaperone Binding In Vivo
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Intrinsically Disordered Proteins Display No Preference for Chaperone Binding In Vivo

机译：本质上紊乱的蛋白质没有伴侣伴侣体内结合的偏好。

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Intrinsically disordered/unstructured proteins (IDPs) are extremely sensitive to proteolysis in vitro, but show no enhanced degradation rates in vivo. Their existence and functioning may be explained if IDPs are preferentially associated with chaperones in the cell, which may offer protection against degradation by proteases. To test this inference, we took pairwise interaction data from high-throughput interaction studies and analyzed to see if predicted disorder correlates with the tendency of chaperone binding by proteins. Our major finding is that disorder predicted by the IUPred algorithm actually shows negative correlation with chaperone binding in E. coli, S. cerevisiae, and metazoa species. Since predicted disorder positively correlates with the tendency of partner binding in the interactome, the difference between the disorder of chaperone-binding and non-binding proteins is even more pronounced if normalized to their overall tendency to be involved in pairwise protein–protein interactions. We argue that chaperone binding is primarily required for folding of globular proteins, as reflected in an increased preference for chaperones of proteins in which at least one Pfam domain exists. In terms of the functional consequences of chaperone binding of mostly disordered proteins, we suggest that its primary reason is not the assistance of folding, but promotion of assembly with partners. In support of this conclusion, we show that IDPs that bind chaperones also tend to bind other proteins.
机译：本质上无序/非结构化的蛋白质（IDP）在体外对蛋白水解极为敏感，但在体内却未显示出增强的降解速率。如果IDP优先与细胞中的伴侣结合，则可以解释它们的存在和功能，这可以提供针对蛋白酶降解的保护。为了检验这一推论，我们从高通量相互作用研究中获取了成对相互作用数据，并进行了分析，以查看预测的疾病是否与蛋白结合伴侣的趋势有关。我们的主要发现是，由IUPred算法预测的疾病实际上显示出与大肠杆菌，酿酒酵母和后生动物物种中分子伴侣结合的负相关性。由于预测的疾病与相互作用组中伴侣结合的趋势呈正相关，因此，如果将分子伴侣结合和非结合蛋白的疾病总体趋势归一化，将其涉及成对的蛋白质-蛋白相互作用，则这种疾病之间的差异就更加明显。我们认为，伴侣蛋白结合是球状蛋白折叠的主要要求，这反映了对其中至少一个Pfam结构域存在的蛋白伴侣蛋白的偏好增加。关于大多数无序蛋白的伴侣结合的功能后果，我们认为其主要原因不是折叠的协助，而是与伴侣的组装的促进。为了支持该结论，我们显示了结合伴侣分子的IDP也倾向于结合其他蛋白质。

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