DOI: 10.1073/pnas.1707385114
论文题名: MinE conformational dynamics regulate membrane binding; MinD interaction; and Min oscillation
作者: Park K.-T. ; Villar M.T. ; Artigues A. ; Lutkenhaus J.
刊名: Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
出版年: 2017
卷: 114, 期: 29 起始页码: 7497
结束页码: 7504
语种: 英语
英文关键词: Conformational dynamics
; Min oscillator
; MinD
; MinE
; Self-organization
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
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. Citation statistics:
资源类型: 期刊论文
标识符: http://119.78.100.158/handle/2HF3EXSE/163814
Appears in Collections: 气候变化与战略
There are no files associated with this item.
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
Recommended Citation:
Park K.-T.,Villar M.T.,Artigues A.,et al. MinE conformational dynamics regulate membrane binding; MinD interaction; and Min oscillation[J]. Proceedings of the National Academy of Sciences of the United States of America,2017-01-01,114(29)