Tarassov Kirill, Messier Vincent, Landry Christian R, Radinovic Stevo, Serna Molina Mercedes M, Shames Igor, Malitskaya Yelena, Vogel Jackie, Bussey Howard, Michnick Stephen W
Département de Biochimie, Université de Montréal Casier postal 6128, Succursale Centre-ville, Montréal, Québec H3C 3J7, Canada.
Science. 2008 Jun 13;320(5882):1465-70. doi: 10.1126/science.1153878. Epub 2008 May 8.
Protein interactions regulate the systems-level behavior of cells; thus, deciphering the structure and dynamics of protein interaction networks in their cellular context is a central goal in biology. We have performed a genome-wide in vivo screen for protein-protein interactions in Saccharomyces cerevisiae by means of a protein-fragment complementation assay (PCA). We identified 2770 interactions among 1124 endogenously expressed proteins. Comparison with previous studies confirmed known interactions, but most were not known, revealing a previously unexplored subspace of the yeast protein interactome. The PCA detected structural and topological relationships between proteins, providing an 8-nanometer-resolution map of dynamically interacting complexes in vivo and extended networks that provide insights into fundamental cellular processes, including cell polarization and autophagy, pathways that are evolutionarily conserved and central to both development and human health.
蛋白质相互作用调节细胞的系统水平行为;因此,在细胞环境中解析蛋白质相互作用网络的结构和动态是生物学的核心目标。我们通过蛋白质片段互补分析(PCA)在酿酒酵母中进行了全基因组范围内的蛋白质-蛋白质相互作用体内筛选。我们鉴定了1124种内源性表达蛋白质之间的2770种相互作用。与先前研究的比较证实了已知的相互作用,但大多数是未知的,揭示了酵母蛋白质相互作用组中一个以前未被探索的子空间。PCA检测到了蛋白质之间的结构和拓扑关系,提供了体内动态相互作用复合物的8纳米分辨率图谱以及扩展网络,这些网络为深入了解基本细胞过程提供了线索,包括细胞极化和自噬,这些途径在进化上是保守的,对发育和人类健康都至关重要。