Large-scale aggregation analysis of eukaryotic proteins reveals an involvement of intrinsically disordered regions in protein folding.
Large-scale aggregation analysis of eukaryotic proteins reveals an involvement of intrinsically disordered regions in protein folding.
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DOI：
10.1038/s41598-017-18977-5
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发表时间：
2018-01-12
影响因子：
4.6
通讯作者：
Taguchi H
中科院分区：
文献类型：
--
作者：
Uemura E;Niwa T;Minami S;Takemoto K;Fukuchi S;Machida K;Imataka H;Ueda T;Ota M;Taguchi H
蛋白质组的一个子集易于聚集形成，这是由细胞中的伴侣蛋白阻止的。为了研究聚集过程的基本原理是否在原核生物和真核生物中是共同的，我们使用无伴侣蛋白重构翻译系统对约500种胞质芽殖酵母蛋白进行了大规模聚集分析，并将获得的数据与先前报道的约3，000种大肠杆菌蛋白进行了比较。虽然影响聚集倾向的理化性质在酵母和E.大肠杆菌蛋白质，酵母蛋白质的聚集的敏感性与固有无序区（IDR）的存在呈正相关。值得注意的是，聚集倾向没有显着改变模型IDR-含蛋白质中的IDR的去除，这表明这些蛋白质中的有序区域的属性是聚集体形成的主导因素。我们还发现，具有较长IDR的蛋白质不受E.大肠杆菌伴侣蛋白GroEL/ES，而细菌和酵母Hsp 70/40伴侣蛋白具有很强的聚集预防作用，即使是具有IDR的蛋白质。这些结果表明，一个关键的决定因素，区分真核生物蛋白质组从原核生物蛋白质组的蛋白质折叠将是连接的IDR。
A subset of the proteome is prone to aggregate formation, which is prevented by chaperones in the cell. To investigate whether the basic principle underlying the aggregation process is common in prokaryotes and eukaryotes, we conducted a large-scale aggregation analysis of ~500 cytosolic budding yeast proteins using a chaperone-free reconstituted translation system, and compared the obtained data with that of ~3,000 Escherichia coli proteins reported previously. Although the physicochemical properties affecting the aggregation propensity were generally similar in yeast and E. coli proteins, the susceptibility of aggregation in yeast proteins were positively correlated with the presence of intrinsically disordered regions (IDRs). Notably, the aggregation propensity was not significantly changed by a removal of IDRs in model IDR-containing proteins, suggesting that the properties of ordered regions in these proteins are the dominant factors for aggregate formation. We also found that the proteins with longer IDRs were disfavored by E. coli chaperonin GroEL/ES, whereas both bacterial and yeast Hsp70/40 chaperones have a strong aggregation-prevention effect even for proteins possessing IDRs. These results imply that a key determinant to discriminate the eukaryotic proteomes from the prokaryotic proteomes in terms of protein folding would be the attachment of IDRs.
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影响因子：
5.6
作者：
Jones, DT
通讯作者：
Jones, DT
影响因子：
--
作者：
Fukuchi S;Hosoda K;Homma K;Gojobori T;Nishikawa K
通讯作者：
Nishikawa K
影响因子：
9.9
作者：
Gong, Yunchen;Kakihara, Yoshito;Krogan, Nevan;Greenblatt, Jack;Emili, Andrew;Zhang, Zhaolei;Houry, Walid A.
通讯作者：
Houry, Walid A.
影响因子：
--
作者：
Fukuchi, Satoshi;Homma, Keiichi;Nishikawa, Ken
通讯作者：
Nishikawa, Ken
影响因子：
14.9
作者：
Kawabata, T;Fukuchi, S;Nishikawa, K
通讯作者：
Nishikawa, K