气候变化领域集成服务门户(CCPortal): The intracellular environment affects protein-protein interactions

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DOI	10.1073/pnas.2019918118
	The intracellular environment affects protein-protein interactions
	Speer S.L.; Zheng W.; Jiang X.; Chu I.-T.; Guseman A.J.; Liu M.; Pielak G.J.; Li C.
发表日期	2021
ISSN	00278424
卷号	118 期号:11
英文摘要	Protein-protein interactions are essential for life but rarely thermodynamically quantified in living cells. In vitro efforts show that protein complex stability is modulated by high concentrations of cosolutes, including synthetic polymers, proteins, and cell lysates via a combination of hard-core repulsions and chemical interactions. We quantified the stability of a model protein complex, the A34F GB1 homodimer, in buffer, Escherichia coli cells and Xenopus laevis oocytes. The complex is more stable in cells than in buffer and more stable in oocytes than E. coli. Studies of several variants show that increasing the negative charge on the homodimer surface increases stability in cells. These data, taken together with the fact that oocytes are less crowded than E. coli cells, lead to the conclusion that chemical interactions aremore important than hard-core repulsions under physiological conditions, a conclusion also gleaned from studies of protein stability in cells. Our studies have implications for understanding how promiscuous-and specific-interactions coherently evolve for a protein to properly function in the crowded cellular environment. © 2021 National Academy of Sciences. All rights reserved.
英文关键词	Macromolecular crowding; Protein; Protein-protein interactions; Thermodynamics
语种	英语
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/180292
作者单位	Department of Chemistry, University of North Carolin1, Chapel Hill, NC 27599, United States; Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan National Laboratory for Optoelectronics, Wuhan Institute of Physics and Mathematics, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences, Wuhan, 430071, China; Graduate University of Chinese Academy of Sciences, Beijing, 100049, China; Department of Biochemistry and Biophysics, University of North Carolin1, Chapel Hill, NC 27599, United States; Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, NC 27599, United States; Integrative Program for Biological and Genome Sciences, University of North Carolina, Chapel Hill, NC 27599, United States
推荐引用方式 GB/T 7714	Speer S.L.,Zheng W.,Jiang X.,et al. The intracellular environment affects protein-protein interactions[J],2021,118(11).
APA	Speer S.L..,Zheng W..,Jiang X..,Chu I.-T..,Guseman A.J..,...&Li C..(2021).The intracellular environment affects protein-protein interactions.Proceedings of the National Academy of Sciences of the United States of America,118(11).
MLA	Speer S.L.,et al."The intracellular environment affects protein-protein interactions".Proceedings of the National Academy of Sciences of the United States of America 118.11(2021).