Itzhaki Zohar, Akiva Eyal, Altuvia Yael, Margalit Hanah
Department of Molecular Genetics and Biotechnology, Faculty of Medicine, The Hebrew University of Jerusalem, Jerusalem 91120, Israel.
Genome Biol. 2006;7(12):R125. doi: 10.1186/gb-2006-7-12-r125.
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.
最近，人们对将结构域-结构域相互作用（DDIs）与蛋白质-蛋白质相互作用（PPIs）联系起来以及反之亦然产生了浓厚兴趣，试图理解PPIs的分子基础。
在此，我们将结构推导的DDIs映射到不同生物体的细胞PPI网络上，并证明存在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DDIs在蛋白质复合物中频繁出现，并且（结构域与自身的）同型相互作用很丰富。对大肠杆菌、酿酒酵母、秀丽隐杆线虫、黑腹果蝇和人类网络中DDIs库的比较表明，许多DDIs在进化上是保守的。
我们的结果表明不同生物体在PPIs中使用相同的“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以维持。
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