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Chiral vortex dynamics on membranes is an intrinsic property of FtsZ, driven by GTP hydrolysis

Diego Ramirez, Daniela A. García-Soriano, Ana Raso, Mario Feingold, Germán Rivas, Petra Schwille
doi: https://doi.org/10.1101/079533
Diego Ramirez
Department of Cellular and Molecular Biophysics, Max Planck Institute for Biochemistry, Martinsried, GermanyGraduate School for Quantitative Biosciences (QBM), Ludwig-Maximillians-University, Munich, Germany
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Daniela A. García-Soriano
Department of Cellular and Molecular Biophysics, Max Planck Institute for Biochemistry, Martinsried, GermanyGraduate School for Quantitative Biosciences (QBM), Ludwig-Maximillians-University, Munich, Germany
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Ana Raso
Department of Cellular and Molecular Biophysics, Max Planck Institute for Biochemistry, Martinsried, GermanyCentro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC), Madrid, Spain
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Mario Feingold
Department of Physics, Ben Gurion University, Beer Sheva, Israel
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Germán Rivas
Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC), Madrid, Spain
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Petra Schwille
Department of Cellular and Molecular Biophysics, Max Planck Institute for Biochemistry, Martinsried, Germany
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  • For correspondence: schwille@biochem.mpg.de
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Abstract

The primary protein of the bacterial Z ring guiding cell division, FtsZ, has recently been shown to engage in intriguing self-organization together with one of its natural membrane anchors, FtsA. When co-reconstituted on flat supported membranes, these proteins assemble into dynamic chiral vortices whose diameters resemble the cell circumference. These dynamics are due to treadmilling polar FtsZ filaments, supposedly destabilized by the co-polymerizing membrane adaptor FtsA, thus catalysing their turnover. Here we show that FtsA is in fact dispensable and that the phenomenon is an intrinsic property of FtsZ alone when supplemented with a membrane anchor. The emergence of these chiral dynamic patterns is critically dependent on GTP concentration and FtsZ surface densities, in agreement with theoretical predictions. The interplay of membrane tethering, GTP binding, and hydrolysis promotes both, the assembly and the destabilization of FtsZ polymers, leading to the observed treadmilling dynamics. Notably, the vortex chirality is defined by the position of the membrane targeting sequence (mts) and can be inverted when attaching it to the opposite end of FtsZ. This reveals a so far unknown vectorial character of these cytomotive filaments, comprising three orthogonal directions: Filament polarity, curvature, and membrane attachment.

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Posted October 07, 2016.
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Chiral vortex dynamics on membranes is an intrinsic property of FtsZ, driven by GTP hydrolysis
Diego Ramirez, Daniela A. García-Soriano, Ana Raso, Mario Feingold, Germán Rivas, Petra Schwille
bioRxiv 079533; doi: https://doi.org/10.1101/079533
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Chiral vortex dynamics on membranes is an intrinsic property of FtsZ, driven by GTP hydrolysis
Diego Ramirez, Daniela A. García-Soriano, Ana Raso, Mario Feingold, Germán Rivas, Petra Schwille
bioRxiv 079533; doi: https://doi.org/10.1101/079533

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