Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Cell. 2011 Oct 28;147(3):690-703. doi: 10.1016/j.cell.2011.08.047.
Determining the composition of protein complexes is an essential step toward understanding the cell as an integrated system. Using coaffinity purification coupled to mass spectrometry analysis, we examined protein associations involving nearly 5,000 individual, FLAG-HA epitope-tagged Drosophila proteins. Stringent analysis of these data, based on a statistical framework designed to define individual protein-protein interactions, led to the generation of a Drosophila protein interaction map (DPiM) encompassing 556 protein complexes. The high quality of the DPiM and its usefulness as a paradigm for metazoan proteomes are apparent from the recovery of many known complexes, significant enrichment for shared functional attributes, and validation in human cells. The DPiM defines potential novel members for several important protein complexes and assigns functional links to 586 protein-coding genes lacking previous experimental annotation. The DPiM represents, to our knowledge, the largest metazoan protein complex map and provides a valuable resource for analysis of protein complex evolution.
确定蛋白质复合物的组成是理解细胞作为一个整体系统的重要步骤。我们使用共亲和纯化结合质谱分析，研究了近 5000 个个体、FLAG-HA 表位标签的果蝇蛋白的蛋白相互作用。基于旨在定义单个蛋白质-蛋白质相互作用的统计框架，对这些数据进行了严格的分析，导致生成了一个包含 556 个蛋白质复合物的果蝇蛋白质相互作用图谱 (DPiM)。DPiM 的高质量及其作为后生动物蛋白质组范例的有用性，从以下几个方面显而易见：回收了许多已知的复合物，显著富集了共享的功能属性，并且在人类细胞中得到了验证。DPiM 为几个重要的蛋白质复合物确定了潜在的新成员，并为 586 个缺乏先前实验注释的蛋白质编码基因赋予了功能联系。据我们所知，DPiM 代表了最大的后生动物蛋白质复合物图谱，为蛋白质复合物进化的分析提供了有价值的资源。
