A large accessory protein interactome is rewired across environments.
A large accessory protein interactome is rewired across environments.
复制标题
DOI：
10.7554/elife.62365
复制
发表时间：
2020-09-14
期刊：
影响因子：
7.7
通讯作者：
Levy SF
中科院分区：
文献类型：
--
作者：
Liu Z;Miller D;Li F;Liu X;Levy SF
To characterize how protein-protein interaction (PPI) networks change, we quantified the relative PPI abundance of 1.6 million protein pairs in the yeast Saccharomyces cerevisiae across nine growth conditions, with replication, for a total of 44 million measurements. Our multi-condition screen identified 13,764 pairwise PPIs, a threefold increase over PPIs identified in one condition. A few ‘immutable’ PPIs are present across all conditions, while most ‘mutable’ PPIs are rarely observed. Immutable PPIs aggregate into highly connected ‘core’ network modules, with most network remodeling occurring within a loosely connected ‘accessory’ module. Mutable PPIs are less likely to co-express, co-localize, and be explained by simple mass action kinetics, and more likely to contain proteins with intrinsically disordered regions, implying that environment-dependent association and binding is critical to cellular adaptation. Our results show that protein interactomes are larger than previously thought and contain highly dynamic regions that reorganize to drive or respond to cellular changes.
