Center for Proteomics and Bioinformatics, Western Reserve University School of Medicine, Cleveland, Ohio 44106, USA.
J Proteome Res. 2012 Sep 7;11(9):4476-87. doi: 10.1021/pr300227y. Epub 2012 Aug 21.
Large-scale protein-protein interaction data sets have been generated for several species including yeast and human and have enabled the identification, quantification, and prediction of cellular molecular networks. Affinity purification-mass spectrometry (AP-MS) is the preeminent methodology for large-scale analysis of protein complexes, performed by immunopurifying a specific "bait" protein and its associated "prey" proteins. The analysis and interpretation of AP-MS data sets is, however, not straightforward. In addition, although yeast AP-MS data sets are relatively comprehensive, current human AP-MS data sets only sparsely cover the human interactome. Here we develop a framework for analysis of AP-MS data sets that addresses the issues of noise, missing data, and sparsity of coverage in the context of a current, real world human AP-MS data set. Our goal is to extend and increase the density of the known human interactome by integrating bait-prey and cocomplexed preys (prey-prey associations) into networks. Our framework incorporates a score for each identified protein, as well as elements of signal processing to improve the confidence of identified protein-protein interactions. We identify many protein networks enriched in known biological processes and functions. In addition, we show that integrated bait-prey and prey-prey interactions can be used to refine network topology and extend known protein networks.
已经为包括酵母和人类在内的几个物种生成了大规模的蛋白质-蛋白质相互作用数据集,这些数据集使细胞分子网络的鉴定、量化和预测成为可能。亲和纯化-质谱(AP-MS)是大规模分析蛋白质复合物的卓越方法,通过免疫纯化特定的“诱饵”蛋白及其相关的“猎物”蛋白来进行。然而,AP-MS 数据集的分析和解释并不简单。此外,尽管酵母 AP-MS 数据集相对全面,但当前的人类 AP-MS 数据集仅稀疏地覆盖了人类相互作用组。在这里,我们开发了一种分析 AP-MS 数据集的框架,该框架解决了当前真实世界人类 AP-MS 数据集中噪声、缺失数据和覆盖稀疏性的问题。我们的目标是通过将诱饵-猎物和共复合物猎物(猎物-猎物关联)整合到网络中,扩展和增加已知的人类相互作用组的密度。我们的框架为每个鉴定的蛋白质分配了一个分数,并结合了信号处理的元素,以提高鉴定的蛋白质-蛋白质相互作用的置信度。我们确定了许多富含已知生物学过程和功能的蛋白质网络。此外,我们还表明,整合的诱饵-猎物和猎物-猎物相互作用可用于细化网络拓扑结构并扩展已知的蛋白质网络。