气候变化领域集成服务门户(CCPortal): MinE conformational dynamics regulate membrane binding; MinD interaction; and Min oscillation

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DOI	10.1073/pnas.1707385114
	MinE conformational dynamics regulate membrane binding; MinD interaction; and Min oscillation
	Park K.-T.; Villar M.T.; Artigues A.; Lutkenhaus J.
发表日期	2017
ISSN	0027-8424
起始页码	7497
结束页码	7504
卷号	114 期号:29
英文摘要	In Escherichia coli MinE induces MinC/MinD to oscillate between the ends of the cell, contributing to the precise placement of the Z ring at midcell. To do this, MinE undergoes a remarkable conformational change from a latent 6β-stranded form that diffuses in the cytoplasm to an active 4β-stranded form bound to the membrane and MinD. How this conformational switch occurs is not known. Here, using hydrogen–deuterium exchange coupled to mass spectrometry (HDX-MS) we rule out a model in which the two forms are in rapid equilibrium. Furthermore, HDX-MS revealed that a MinE mutant (D45A/V49A), previously shown to produce an aberrant oscillation and unable to assemble a MinE ring, is more rigid than WT MinE. This mutant has a defect in interaction with MinD, suggesting it has difficulty in switching to the active form. Analysis of intragenic suppressors of this mutant suggests it has difficulty in releasing the N-terminal membrane targeting sequences (MTS). These results indicate that the dynamic association of the MTS with the β-sheet is fine-tuned to balance MinE’s need to sense MinD on the membrane with its need to diffuse in the cytoplasm, both of which are necessary for the oscillation. The results lead to models for MinE activation and MinE ring formation. © 2017, National Academy of Sciences. All rights reserved.
英文关键词	Conformational dynamics; Min oscillator; MinD; MinE; Self-organization
语种	英语
scopus关键词	bacterial protein; deuterium; hydrogen; MinD protein; protein min; protein mine; unclassified drug; adenosine triphosphatase; cell cycle protein; Escherichia coli protein; membrane protein; MinC protein, E coli; MinD protein, E coli; MinE protein, E coli; peptide; protein binding; amino terminal sequence; Article; beta sheet; conformational transition; cytoplasm; Escherichia coli; mass spectrometry; membrane binding; nonhuman; priority journal; protein interaction; chemistry; metabolism; mutation; oscillometry; phenotype; plasmid; protein multimerization; protein secondary structure; Adenosine Triphosphatases; Cell Cycle Proteins; Deuterium; Escherichia coli; Escherichia coli Proteins; Hydrogen; Membrane Proteins; Mutation; Oscillometry; Peptides; Phenotype; Plasmids; Protein Binding; Protein Multimerization; Protein Structure, Secondary
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/160611
作者单位	Park, K.-T., Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Kansas City, KS 66160, United States; Villar, M.T., Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS 66160, United States; Artigues, A., Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS 66160, United States; Lutkenhaus, J., Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Kansas City, KS 66160, United States
推荐引用方式 GB/T 7714	Park K.-T.,Villar M.T.,Artigues A.,et al. MinE conformational dynamics regulate membrane binding; MinD interaction; and Min oscillation[J],2017,114(29).
APA	Park K.-T.,Villar M.T.,Artigues A.,&Lutkenhaus J..(2017).MinE conformational dynamics regulate membrane binding; MinD interaction; and Min oscillation.Proceedings of the National Academy of Sciences of the United States of America,114(29).
MLA	Park K.-T.,et al."MinE conformational dynamics regulate membrane binding; MinD interaction; and Min oscillation".Proceedings of the National Academy of Sciences of the United States of America 114.29(2017).