Structural disorder promotes assembly of protein complexes.
Structural disorder promotes assembly of protein complexes.
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DOI：
10.1186/1472-6807-7-65
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发表时间：
2007-10-08
影响因子：
--
通讯作者：
Tompa P
中科院分区：
文献类型：
--
作者：
Hegyi H;Schad E;Tompa P
蛋白质复合物的组装与蛋白质紊乱有关的观点仅从少数大型复合物（如病毒衣壳或细菌鞭毛系统）中推断出来。这种关系表明，更大的情结有更多的紊乱，但从未被系统地测试过。最近对细胞中蛋白质-蛋白质相互作用和蛋白质复合物的高通量分析产生了能够通过生物信息学手段解决这一问题的数据。在这项工作中，我们预测了大肠杆菌和酿酒杆菌的结构紊乱，并将其与复合物的大小相关联。使用iuppred预测每个复合物的紊乱，我们发现紊乱与组装成复合物的蛋白质数量之间存在统计学上显著的相关性。在酵母中，2-4组分复合物的无序分布中值为10%（在大肠杆菌中为6%），但在11-100蛋白的复合物中为18%（在大肠杆菌中为12%）。对超过30个连续无序残基的区域进行的无序程度评估显示，小复合体和大复合体之间的分裂甚至更强（酵母中2-4个组分的复合体的中值约为4%，而11-100个组分的复合体的中值为12%）。预测的相关性也得到了实验证据的支持，通过观察在蛋白质数据库中可以找到的复合物的蛋白质成分的结构紊乱(中位数为1。酵母中2-4组分的配合物为5%，11-100组分的配合物为9.6%)。进一步的分析表明，这种相关性与中心蛋白紊乱的增加没有直接联系，而是反映了构成复合物的蛋白质的真正系统特性。总之，我们提出并讨论了蛋白质复合物的组装是由蛋白质紊乱激活并可能促进的。
The idea that the assembly of protein complexes is linked with protein disorder has been inferred from a few large complexes, such as the viral capsid or bacterial flagellar system, only. The relationship, which suggests that larger complexes have more disorder, has never been systematically tested. The recent high-throughput analyses of protein-protein interactions and protein complexes in the cell generated data that enable to address this issue by bioinformatic means. In this work we predicted structural disorder for both E. coli and S. cerevisiae, and correlated it with the size of complexes. Using IUPred to predict the disorder for each complex, we found a statistically significant correlation between disorder and the number of proteins assembled into complexes. The distribution of disorder has a median value of 10% in yeast for complexes of 2–4 components (6% in E. coli), but 18% for complexes in the size range of 11–100 proteins (12% in E. coli). The level of disorder as assessed for regions longer than 30 consecutive disordered residues shows an even stronger division between small and large complexes (median values about 4% for complexes of 2–4 components, but 12% for complexes of 11–100 components in yeast). The predicted correlation is also supported by experimental evidence, by observing the structural disorder in protein components of complexes that can be found in the Protein Data Bank (median values 1. 5% for complexes of 2–4 components, and 9.6% for complexes of 11–100 components in yeast). Further analysis shows that this correlation is not directly linked with the increased disorder in hub proteins, but reflects a genuine systemic property of the proteins that make up the complexes. Overall, it is suggested and discussed that the assembly of protein-protein complexes is enabled and probably promoted by protein disorder.
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Ekman D;Light S;Björklund AK;Elofsson A
通讯作者：
Elofsson A
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64.8
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Gavin, AC;Bösche, M;Superti-Furga, G
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Superti-Furga, G
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64.8
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