《自然》（Nature 415: 6868 10 January 2002）雜志發(fā)表了來自兩個小組的關(guān)于酵母Saccharomyces cerevisiae的大規(guī)模功能蛋白學(xué)研究結(jié)果。第一個小組所進(jìn)行的是Cellzome,、EMBL和CGM-CNRS三個機(jī)構(gòu)之間的一項合作研究,，共有超過1700個蛋白通過同源重組得以標(biāo)記,，其中1143個與人體生物學(xué)有關(guān),。對基因產(chǎn)物的質(zhì)譜研究識別出了232個多蛋白復(fù)合物,，還識別出344種蛋白的新的細(xì)胞功能,。另一個小組的成員包括來自MDS Proteomics及三個加拿大研究機(jī)構(gòu)的科學(xué)家,，他們分析了所預(yù)測出的作為誘餌的酵母蛋白中的10%以上,，檢測出占該基因組25%的3617種相關(guān)蛋白,。
Functional organization of the yeast proteome by systematic analysis
of protein complexes
Most cellular processes are carried out by multiprotein complexes. The identification and analysis of their components provides insight into how the ensemble of expressed proteins (proteome) is organized into functional units. We used tandem-affinity purification (TAP) and mass spectrometry in a large-scale approach to characterize multiprotein complexes in Saccharomyces cerevisiae. We processed 1,739 genes, including 1,143 human orthologues of relevance to human biology, and purified 589 protein assemblies. Bioinformatic analysis of these assemblies defined 232 distinct multiprotein complexes and proposed new cellular roles for 344 proteins, including 231 proteins with no previous functional annotation. Comparison of yeast and human complexes showed that conservation across species extends from single proteins to their molecular environment. Our analysis provides an outline of the eukaryotic proteome as a network of protein complexes at a level of organization beyond binary interactions. This higher-order map contains fundamental biological information and offers the context for a more reasoned and informed approach to drug discovery.
