Department of Chemistry, Washington State University, Pullman, WA 99164, USA.
Mol Cell Proteomics. 2011 Oct;10(10):M110.006841. doi: 10.1074/mcp.M110.006841. Epub 2011 Jun 22.
Identification and measurement of in vivo protein interactions pose critical challenges in the goal to understand biological systems. The measurement of structures and topologies of proteins and protein complexes as they exist in cells is particularly challenging, yet critically important to improve understanding of biological function because proteins exert their intended function only through the structures and interactions they exhibit in vivo. In the present study, protein interactions in E. coli cells were identified in our unbiased cross-linking approach, yielding the first in vivo topological data on many interactions and the largest set of identified in vivo cross-linked peptides produced to date. These data show excellent agreement with protein and complex crystal structures where available. Furthermore, our unbiased data provide novel in vivo topological information that can impact understanding of biological function, even for cases where high resolution structures are not yet available.
在了解生物系统的目标中，鉴定和测量体内蛋白质相互作用提出了重大挑战。测量蛋白质和蛋白质复合物在细胞中存在的结构和拓扑结构特别具有挑战性，但对于提高对生物功能的理解至关重要，因为蛋白质只有通过它们在体内表现出的结构和相互作用才能发挥其预期的功能。在本研究中，我们通过无偏交联方法鉴定了大肠杆菌细胞中的蛋白质相互作用，获得了许多相互作用的第一个体内拓扑数据，以及迄今为止产生的最大一组鉴定的体内交联肽。这些数据与可用的蛋白质和复合物晶体结构非常吻合。此外，我们的无偏数据提供了新的体内拓扑信息，即使对于那些尚未获得高分辨率结构的情况，也可能影响对生物功能的理解。
