Peeling the yeast protein network
Peeling the yeast protein network
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DOI：
10.1002/pmic.200400962
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发表时间：
2005-02-01
期刊：
影响因子：
3.4
通讯作者：
Almaas, E
中科院分区：
文献类型：
--
作者：
Wuchty, S;Almaas, E
一组高度连接的蛋白质(或中枢)通过连接酿酒酵母蛋白质相互作用网络的固有模块对该网络的完整性起着重要作用[1，2]。这些枢纽的中心位置的重要性进一步被它们致命的倾向所证实。然而，尽管得到了高度重视，但人们对中枢之间的拓扑一致性知之甚少。应用一种核心分解方法，使我们能够识别蛋白质相互作用网络的固有层结构，我们发现，节点被基本和进化保守的概率向最内层的核心依次增加。虽然连通性本身通常不是评估蛋白质功能、进化和拓扑相关性的充分标准，但我们根据节点在内核或外核的外观将节点归类为全局和局部中心。全球中心蛋白质参与了大量的蛋白质复合体，这些蛋白质复合体表现出高度的进化保守性，这使得我们可以假设全球中心蛋白质是蛋白质组的进化脊梁。尽管蛋白质相互作用数据有很大的缺陷，我们发现我们的结果对于不准确确定的蛋白质相互作用是非常稳健的。
A set of highly connected proteins (or hubs) plays an important role for the integrity of the protein interaction network of Saccharomyces cerevisae by connecting the network's intrinsic modules [1, 2]. The importance of the hubs' central placement is further confirmed by their propensity to be lethal. However, although highly emphasized, little is known about the topological coherence among the hubs. Applying a core decomposition method which allows us to identify the inherent layer structure of the protein interaction network, we find that the probability of nodes both being essential and evolutionary conserved successively increases toward the innermost cores. While connectivity alone is often not a sufficient criterion to assess a protein's functional, evolutionary and topological relevance, we classify nodes as globally and locally central depending on their appearance in the inner or outer cores. The observation that globally central proteins participate in a substantial number of protein complexes which display an elevated degree of evolutionary conservation allows us to hypothesize that globally central proteins serve as the evolutionary backbone of the proteome. Even though protein interaction data are extensively flawed, we find that our results are very robust against inaccurately determined protein interactions.