气候变化领域集成服务门户(CCPortal): MinE conformational switching confers robustness on self-organized Min protein patterns

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DOI	10.1073/pnas.1719801115
	MinE conformational switching confers robustness on self-organized Min protein patterns
	Denk J.; Kretschmer S.; Halatek J.; Hartl C.; Schwille P.; Frey E.
发表日期	2018
ISSN	0027-8424
起始页码	4553
结束页码	4558
卷号	115 期号:18
英文摘要	Protein patterning is vital for many fundamental cellular processes. This raises two intriguing questions: Can such intrinsically complex processes be reduced to certain core principles and, if so, what roles do the molecular details play in individual systems? A prototypical example for protein patterning is the bacterial Min system, in which self-organized pole-to-pole oscillations of MinCDE proteins guide the cell division machinery to midcell. These oscillations are based on cycling of the ATPase MinD and its activating protein MinE between the membrane and the cytoplasm. Recent biochemical evidence suggests that MinE undergoes a reversible, MinD-dependent conformational switch from a latent to a reactive state. However, the functional relevance of this switch for the Min network and pattern formation remains unclear. By combining mathematical modeling and in vitro reconstitution of mutant proteins, we dissect the two aspects of MinE’s switch, persistent membrane binding and a change in MinE’s affinity for MinD. Our study shows that the MinD-dependent change in MinE’s binding affinity for MinD is essential for patterns to emerge over a broad and physiological range of protein concentrations. Mechanistically, our results suggest that conformational switching of an ATPase-activating protein can lead to the spatial separation of its distinct functional states and thereby confer robustness on an intracellular protein network with vital roles in bacterial cell division. © 2018 National Academy of Sciences. All rights reserved.
英文关键词	conformational switching; in vitro reconstitution; Min system; pattern formation; protein reaction–diffusion networks
语种	英语
scopus关键词	adenosine triphosphatase; bacterial protein; MinD protein; protein MinE; unclassified drug; adenosine triphosphatase; adenosine triphosphate; cell cycle protein; Escherichia coli protein; membrane protein; MinD protein, E coli; MinE protein, E coli; protein binding; Article; bacterial cell; binding affinity; cell division; conformational transition; Escherichia coli; in vitro study; mathematical model; membrane binding; nonhuman; oscillation; priority journal; protein analysis; cell membrane; conformation; cytoplasm; genetics; metabolism; physiology; theoretical model; Adenosine Triphosphatases; Adenosine Triphosphate; Cell Cycle Proteins; Cell Division; Cell Membrane; Cytoplasm; Escherichia coli; Escherichia coli Proteins; Membrane Proteins; Models, Theoretical; Molecular Conformation; Protein Binding
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/160523
作者单位	Denk, J., Arnold-Sommerfeld-Center for Theoretical Physics, Center for NanoScience, Ludwig-Maximilians-Universität München, München, D-80333, Germany; Kretschmer, S., Department of Cellular and Molecular Biophysics, Max-Planck-Institute of Biochemistry, Martinsried, D-82152, Germany; Halatek, J., Arnold-Sommerfeld-Center for Theoretical Physics, Center for NanoScience, Ludwig-Maximilians-Universität München, München, D-80333, Germany; Hartl, C., Arnold-Sommerfeld-Center for Theoretical Physics, Center for NanoScience, Ludwig-Maximilians-Universität München, München, D-80333, Germany; Schwille, P., Department of Cellular and Molecular Biophysics, Max-Planck-Institute of Biochemistry, Martinsried, D-82152, Germany; Frey, E., Arnold-Sommerfeld-Center for Theoretical Physics, Center for NanoScience, Ludwig-Maximilians-Universität München, München, D-80333, Germany
推荐引用方式 GB/T 7714	Denk J.,Kretschmer S.,Halatek J.,et al. MinE conformational switching confers robustness on self-organized Min protein patterns[J],2018,115(18).
APA	Denk J.,Kretschmer S.,Halatek J.,Hartl C.,Schwille P.,&Frey E..(2018).MinE conformational switching confers robustness on self-organized Min protein patterns.Proceedings of the National Academy of Sciences of the United States of America,115(18).
MLA	Denk J.,et al."MinE conformational switching confers robustness on self-organized Min protein patterns".Proceedings of the National Academy of Sciences of the United States of America 115.18(2018).