Why do essential proteins tend to be clustered in the yeast interactome network?
Why do essential proteins tend to be clustered in the yeast interactome network?
复制标题
为什么必需蛋白质往往聚集在酵母相互作用组网络中？
DOI：
10.1039/b921069e
复制
发表时间：
2010-05-01
影响因子：
--
通讯作者：
Luo, Z. W.
中科院分区：
文献类型：
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作者：
Lu, Chenqi;Hu, Xiaohua;Luo, Z. W.
最近，关于中心性-致死性规则的争论被酵母相互作用组网络的“第二代”高通量Y2H数据解决了，这表明蛋白质的连通程度和必要性之间没有显着相关性。然而，目前尚不清楚为什么必需蛋白质强烈倾向于彼此相互作用。此前，提出了必需蛋白质-蛋白质相互作用的概念来解释必需蛋白质聚集的机制。在本文中，我们表明，酵母相互作用组网络中必需蛋白 (IBEP) 之间的过度相互作用 67% 至 75% 可归因于蛋白质复合物内的相互作用，其特征在于复合物内亚基的相同删除表型。此外，IBEP 中 20% 至 78% 的过量是由网络的强模块化结构以及模块之间蛋白质必需性的变化引起的。蛋白质不仅在细胞过程中充当交互网络，而且许多蛋白质并不单独参与网络，而是整合到蛋白质复合物中，并且许多功能相关的复合物整合到模块中。因此，蛋白质复合物的局部结构作为功能模块和结构模块是必需蛋白质聚集的主要影响因素。
Recently, the debate on the centrality-lethality rule is resolved by the "second-generation" high-throughput Y2H data from the yeast interactome network, which suggests no significant correlation between the degree of connectedness and essentiality of proteins. However, it is still not clear why essential proteins strongly tend to interact with each other. Previously, the concept of essential protein-protein interactions was proposed to explain the mechanism underlying the clustering of essential proteins. In this article we show that 67 to 75% of the excessive interactions between essential proteins (IBEPs) in the yeast interactome network can be attributed to interactions within protein complexes characterised by the same deletion phenotype for subunits within the complex. Furthermore, 20 to 78% of the excess in IBEPs are caused by the strongly modular structure of the network and by variation in protein essentiality among modules. Not only do proteins function as an interactive network in cellular processes, but furthermore, many proteins do not take part in the network alone, but integrate into protein complexes and many functionally related complexes integrate into modules. So, the local structure of protein complexes as both functional and structural modules are the main contributory factors in the clustering of essential proteins.