Comprehensive analysis of the effects of Escherichia coli ORFs on protein translation reaction
Comprehensive analysis of the effects of Escherichia coli ORFs on protein translation reaction
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DOI：
10.1074/mcp.m800051-mcp200
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发表时间：
2008-08-01
影响因子：
7
通讯作者：
Yomo, Tetsuya
中科院分区：
文献类型：
--
作者：
Kazuta, Yasuaki;Adachi, Jiro;Yomo, Tetsuya
蛋白质合成是细胞中最重要的反应之一。最近的实验研究表明，通过使用这些单独高度纯化的蛋白质成分重建基于大肠杆菌的体外翻译系统，可以用最少 36 种蛋白质和核糖体的补充来实现这种复杂的反应。根据大肠杆菌蛋白质的蛋白质-蛋白质相互作用 (PPI) 网络，已知这些最小的蛋白质成分会与大量蛋白质发生物理相互作用。然而，目前尚不清楚大肠杆菌蛋白的哪一部分与最小蛋白合成系统在功能上相关。我们研究了每种 4194 个大肠杆菌 ORF 产品对最小蛋白质合成系统的影响；整个 ORF 产物的至少 12%（大肠杆菌基因产物的很大一部分）影响该系统的活性。此外，通过映射显示，PPI 网络中存在的这些功能修饰剂中有 34% 与 PPI 网络的最小组件直接连接（即物理相互作用）。对 PPI 网络中修饰符和最小组件之间关系的拓扑分析表明最小组件的聚类。修饰剂没有表现出这样的聚集，这表明功能修饰剂的位置分布在整个 PPI 网络中，而不是聚集在靠近最小蛋白质成分的地方。这些观察结果可能反映了蛋白质合成系统的进化过程。
Protein synthesis is one of the most important reactions in the cell. Recent experimental studies indicated that this complex reaction can be achieved with a minimum complement of 36 proteins and ribosomes by reconstituting an Escherichia coli-based in vitro translation system with these protein components highly purified on an individual basis. From the protein-protein interaction (PPI) network of E. coli proteins, these minimal protein components are known to interact physically with large numbers of proteins. However, it is unclear what fraction of E. coli proteins are linked functionally with the minimal protein synthesis system. We investigated the effects of each of the 4194 E. coli ORF products on the minimal protein synthesis system; at least 12% of the entire ORF products, a significant fraction of the gene product of E. coli, affect the activity of this system. Furthermore 34% of these functional modifiers present in the PPI network were shown by mapping to be directly linked (i.e. to interact physically) with the minimal components of the PPI network. Topological analysis of the relationships between modifiers and the minimal components in the PPI network indicated clustering of the minimal components. The modifiers showed no such clustering, indicating that the location of functional modifiers is spread across the PPI network rather than clustering close to the minimal protein components. These observations may reflect the evolutionary process of the protein synthesis system.