GroEL binds artificial proteins with random sequences
GroEL binds artificial proteins with random sequences
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DOI：
10.1074/jbc.275.18.13755
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发表时间：
2000-05-05
影响因子：
4.8
通讯作者：
Yoshida, M
中科院分区：
文献类型：
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作者：
Aoki, K;Motojima, F;Yoshida, M
来自大肠杆菌的伴侣蛋白GroEL与许多不相关的蛋白质的非天然状态结合，并且GroEL可识别的结构特征一直存在争议。作为GroEL的模型底物蛋白，我们使用了7个人工蛋白（138个类似于141个残基），每个蛋白都有一个独特但随机选择的氨基酸序列，并且没有折叠成特定结构的倾向。其中2种为水溶性，其余溶于3 M尿素。可溶性的与GroEL相互作用的方式与天然底物相似；刺激GroEL和GroEL/ GroES的atp酶循环，抑制GroEL辅助的其他蛋白质折叠。7种人造蛋白均能与GroEL结合，表明底物蛋白的二级结构和特定序列基序不需要被GroEL识别。
Chaperonin GroEL from Escherichia coli binds to the non-native states of many unrelated proteins, and GroEL-recognizable structural features have been argued. As model substrate proteins of GroEL, we used seven artificial proteins (138 similar to 141 residues), each of which has a unique but randomly chosen amino acid sequence and no propensity to fold into a certain structure. Two of them were water-soluble, and the rest were soluble in 3 M urea. The soluble ones interacted with GroEL in a manner similar to that of a natural substrate; they stimulated the ATPase cycle of GroEL and GroEL/ GroES and inhibited GroEL-assisted folding of other protein. All seven artificial proteins were able to bind to GroEL, The results suggest that the secondary structure as well as the specific sequence motif of the substrate proteins are not necessary to be recognized by GroEL.