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  Treadmilling analysis reveals new insights into dynamic FtsZ ring architecture

Ramirez-Diaz, D. A., Garcia-Soriano, D., Raso, A., Mücksch, J., Feingold, M., Rivas, G., et al. (2018). Treadmilling analysis reveals new insights into dynamic FtsZ ring architecture. PLoS Biology, 16(5): e2004845. doi:10.1371/journal.pbio.2004845.

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Ramirez-Diaz, Diego A.1, Author              
Garcia-Soriano, Daniela1, Author              
Raso, Ana1, Author              
Mücksch, Jonas1, Author              
Feingold, Mario2, Author
Rivas, German2, Author
Schwille, Petra1, Author              
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1Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565169              
2External Organizations, ou_persistent22              

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 Abstract: FtsZ, the primary protein of the bacterial Z ring guiding cell division, has been recently shown to engage in intriguing treadmilling dynamics along the circumference of the division plane. When coreconstituted in vitro with FtsA, one of its natural membrane anchors, on flat supported membranes, these proteins assemble into dynamic chiral vortices compatible with treadmilling of curved polar filaments. Replacing FtsA by a membrane-targeting sequence (mts) to FtsZ, we have discovered conditions for the formation of dynamic rings, showing that the phenomenon is intrinsic to FtsZ. Ring formation is only observed for a narrow range of protein concentrations at the bilayer, which is highly modulated by free Mg2+ and depends upon guanosine triphosphate (GTP) hydrolysis. Interestingly, the direction of rotation can be reversed by switching the mts from the C-terminus to the N-terminus of the protein, implying that the filament attachment must have a perpendicular component to both curvature and polarity. Remarkably, this chirality switch concurs with previously shown inward or outward membrane deformations by the respective FtsZ mutants. Our results lead us to suggest an intrinsic helicity of FtsZ filaments with more than one direction of curvature, supporting earlier hypotheses and experimental evidence.

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 Dates: 2018
 Publication Status: Published online
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 Rev. Type: Peer
 Identifiers: DOI: 10.1371/journal.pbio.2004845
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Title: PLoS Biology
  Other : PLoS Biol.
Source Genre: Journal
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Publ. Info: San Francisco, California, US : Public Library of Science
Pages: - Volume / Issue: 16 (5) Sequence Number: e2004845 Start / End Page: - Identifier: ISSN: 1544-9173
CoNE: https://pure.mpg.de/cone/journals/resource/111056649444170