Bartel P L, Roecklein J A, SenGupta D, Fields S
Department of Molecular Genetics and Microbiology, State University of New York at Stony Brook 11794, USA.
Nat Genet. 1996 Jan;12(1):72-7. doi: 10.1038/ng0196-72.
Genome sequencing projects are predicting large numbers of novel proteins, whose interactions with other proteins must mediate the function of cellular processes. To analyse these networks, we used the yeast two-hybrid system on a genome-wide scale to identify 25 interactions among the proteins of Escherichia coli bacteriophage T7. Among these is a set of six interactions connecting proteins that function in DNA replication and DNA packaging. Remarkably, two genes, arranged such that one entirely overlaps the other and uses a different reading frame, encode interacting proteins. Several of the interactions reflect intramolecular associations of different domains of the same polypeptide, suggesting that the two-hybrid assay may be useful in the analysis of protein folding. This global approach to protein-protein interactions may be applicable to the analysis of more complex genomes whose sequences are becoming available.
基因组测序项目预测出大量新蛋白质，这些蛋白质与其他蛋白质的相互作用必定介导细胞过程的功能。为了分析这些网络，我们在全基因组规模上使用酵母双杂交系统，以鉴定大肠杆菌噬菌体T7蛋白质之间的25种相互作用。其中有一组六种相互作用，连接了在DNA复制和DNA包装中起作用的蛋白质。值得注意的是，有两个基因的排列方式是一个基因完全重叠另一个基因，并使用不同的阅读框，它们编码相互作用的蛋白质。其中一些相互作用反映了同一多肽不同结构域的分子内关联，这表明双杂交分析可能有助于蛋白质折叠的分析。这种研究蛋白质-蛋白质相互作用的全局方法可能适用于对序列已可得的更复杂基因组的分析。
