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  MinE conformational switching confers robustness on self-organized Min protein patterns

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), 4553-4558. doi:10.1073/pnas.1719801115.

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© 2018 the Author(s). Published by PNAS. This open access article is distributed under Creative Commons Attribution-NonCommercial-NoDerivatives License 4.0 (CC BY-NC-ND).

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 Creators:
Denk, Jonas1, Author
Kretschmer, Simon2, Author              
Halatek, Jacob1, Author
Hartl, Caroline1, Author
Schwille, Petra2, Author              
Frey, Erwin1, Author
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1external, ou_persistent22              
2Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565169              

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Free keywords: BACTERIAL-CELL DIVISION; ESCHERICHIA-COLI; REGULATOR MINE; IN-VITRO; CIRCADIAN OSCILLATOR; MEMBRANE INTERACTION; DYNAMICS; LOCALIZATION; BINDING; MODELScience & Technology - Other Topics; Min system; pattern formation; protein reaction-diffusion networks; conformational switching; in vitro reconstitution;
 Abstract: 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.

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Language(s): eng - English
 Dates: 2018
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000431119600034
DOI: 10.1073/pnas.1719801115
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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : Proceedings of the National Academy of Sciences of the USA
  Other : Proc. Acad. Sci. USA
  Other : Proc. Acad. Sci. U.S.A.
  Abbreviation : PNAS
Source Genre: Journal
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Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 115 (18) Sequence Number: - Start / End Page: 4553 - 4558 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230