The protein-protein interaction map of Helicobacter pylori
The protein-protein interaction map of Helicobacter pylori
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DOI：
10.1038/35051615
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发表时间：
2001-01-11
期刊：
影响因子：
64.8
通讯作者：
Legrain, P
中科院分区：
文献类型：
--
作者：
Rain, JC;Selig, L;Legrain, P
随着许多原核和真核基因组的完整DNA序列的可用性，以及很快人类基因组本身的可用性，重要的是要开发可靠的蛋白质组范围的方法，以更好地了解蛋白质的功能（1）。蛋白质间相互作用作为细胞蛋白质复合物和蛋白质通路的基本组成部分，是决定蛋白质功能的关键因素。在这里，我们已经建立了一个大规模的蛋白质-蛋白质相互作用的人类胃病原体幽门螺杆菌的地图。我们采用酵母双杂交的高通量策略筛选261 H。pylori蛋白质与高度复杂的基因组编码多肽文库的比较（2）。在H. pylori蛋白质，连接46.6%的蛋白质组。每一个单一的蛋白质-蛋白质相互作用的可靠性得分的确定和实际的相互作用域的识别允许分配的未注释的蛋白质的生物途径。
With the availability of complete DNA sequences for many prokaryotic and eukaryotic genomes, and soon for the human genome itself, it is important to develop reliable proteome-wide approaches for a better understanding of protein function(1). As elementary constituents of cellular protein complexes and pathways, protein-protein interactions are key determinants of protein function. Here we have built a large-scale protein-protein interaction map of the human gastric pathogen Helicobacter pylori. We have used a high-throughput strategy of the yeast two-hybrid assay to screen 261 H. pylori proteins against a highly complex library of genome-encoded polypeptides(2). Over 1,200 interactions were identired between H. pylori proteins, connecting 46.6% of the proteome. The determination of a reliability score for every single protein-protein interaction and the identification of the actual interacting domains permitted the assignment of unannotated proteins to biological pathways.