Evolutionary conservation of domain-domain interactions.
Evolutionary conservation of domain-domain interactions.
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DOI：
10.1186/gb-2006-7-12-r125
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发表时间：
2006
期刊：
影响因子：
12.3
通讯作者：
Margalit H
中科院分区：
文献类型：
--
作者：
Itzhaki Z;Akiva E;Altuvia Y;Margalit H
将结构域-结构域相互作用映射到不同生物体的细胞蛋白质-蛋白质相互作用网络上表明，存在用于介导细胞中各种相互作用的结构域对目录。最近，人们对将结构域-结构域相互作用（DDI）与蛋白质-蛋白质相互作用（PPI）相关联以及反之亦然产生了很大兴趣，试图理解PPI的分子基础。在这里，我们将结构衍生的DDI映射到不同生物体的细胞PPI网络上，并证明存在一个用于介导细胞中各种相互作用的结构域对目录。我们表明，这些DDI经常发生在蛋白质复合物和同型相互作用（与自身的域）是丰富的。对大肠杆菌、酿酒酵母、秀丽隐杆线虫、黑腹果蝇和智人网络中的DDI库的比较表明，许多DDI在进化上是保守的。我们的结果表明，不同的生物体使用相同的PPI“构建模块”，这表明许多结构域对在介导蛋白质相互作用中的功能在进化中得到了维持。
Mapping of domain-domain interactions onto the cellular protein-protein interaction networks of different organisms demonstrates that there is a catalogue of domain pairs that is used for mediating various interactions in the cell Recently, there has been much interest in relating domain-domain interactions (DDIs) to protein-protein interactions (PPIs) and vice versa, in an attempt to understand the molecular basis of PPIs. Here we map structurally derived DDIs onto the cellular PPI networks of different organisms and demonstrate that there is a catalog of domain pairs that is used to mediate various interactions in the cell. We show that these DDIs occur frequently in protein complexes and that homotypic interactions (of a domain with itself) are abundant. A comparison of the repertoires of DDIs in the networks of Escherichia coli, Saccharomyces cerevisiae, Caenorhabditis elegans, Drosophila melanogaster, and Homo sapiens shows that many DDIs are evolutionarily conserved. Our results indicate that different organisms use the same 'building blocks' for PPIs, suggesting that the functionality of many domain pairs in mediating protein interactions is maintained in evolution.