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MinE conformational dynamics regulate membrane binding, MinD interaction, and Min oscillation

delete2017-06-26
delete36
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OA
AI
K
Kyung‐Tae Park
M
María T. Villar
A
Antonio Artigues
J
Joe Lutkenhaus *
DOI:10.1073/pnas.1707385114delete
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摘要

摘要

En 中文
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 6 beta-stranded form that diffuses in the cytoplasm to an active 4 beta-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 beta-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.
Keyword:
Min oscillator
MinE
MinD
conformational dynamics
self-organization
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期刊

P
Proceedings of the National Academy of Sciences of the United States of America
IF:
9.1
论文数:
10.8W
被引数:
73.5W

机构

U
university of kansas medical center
学者数:
6.5K
论文数: 5.0K
被引数: 6
U
University of Kansas
学者数:
1.9W
论文数: 1.7W
被引数: 8.1K
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Protein Self-Organization: Lessons from the Min System
err2011-06-09
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PREAI
errLoose, Martin; Kruse, Karsten; Schwille, Petra
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