FtsZ induces membrane deformations via torsional stress upon GTP hydrolysis

FtsZ induces membrane deformations via torsional stress upon GTP hydrolysis

During bacterial cell division, the protein FtsZ is the main component of the contractile ring, though how precisely FtsZ treadmilling and its ability to deform membranes cooperate are unclear. Here, the authors show that dynamic FtsZ may deform lipid membranes via torsional stress that may provide...

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Main Authors: Diego A. Ramirez-Diaz, Adrián Merino-Salomón, Fabian Meyer, Michael Heymann, Germán Rivas, Marc Bramkamp, Petra Schwille
Format: Article
Language:English
Published: Nature Publishing Group 2021-06-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-021-23387-3
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spelling doaj-6bb71fb019714b2eacacc1d99a61c0c22021-06-06T11:14:11ZengNature Publishing GroupNature Communications2041-17232021-06-0112111110.1038/s41467-021-23387-3FtsZ induces membrane deformations via torsional stress upon GTP hydrolysisDiego A. Ramirez-Diaz0Adrián Merino-Salomón1Fabian Meyer2Michael Heymann3Germán Rivas4Marc Bramkamp5Petra Schwille6Department of Cellular and Molecular Biophysics, Max Planck Institute of BiochemistryDepartment of Cellular and Molecular Biophysics, Max Planck Institute of BiochemistryInstitute of General Microbiology, Christian-Albrechts-UnversityDepartment of Cellular and Molecular Biophysics, Max Planck Institute of BiochemistryCentro de Investigaciones Biológicas Margarita Salas, Consejo Superior de Investigaciones Cientificas (CSIC)Institute of General Microbiology, Christian-Albrechts-UnversityDepartment of Cellular and Molecular Biophysics, Max Planck Institute of BiochemistryDuring bacterial cell division, the protein FtsZ is the main component of the contractile ring, though how precisely FtsZ treadmilling and its ability to deform membranes cooperate are unclear. Here, the authors show that dynamic FtsZ may deform lipid membranes via torsional stress that may provide sufficient force to constrict membranes in vivo and in vitro.https://doi.org/10.1038/s41467-021-23387-3
collection DOAJ
language English
format Article
sources DOAJ
author Diego A. Ramirez-Diaz
Adrián Merino-Salomón
Fabian Meyer
Michael Heymann
Germán Rivas
Marc Bramkamp
Petra Schwille
spellingShingle Diego A. Ramirez-Diaz
Adrián Merino-Salomón
Fabian Meyer
Michael Heymann
Germán Rivas
Marc Bramkamp
Petra Schwille
FtsZ induces membrane deformations via torsional stress upon GTP hydrolysis
Nature Communications
author_facet Diego A. Ramirez-Diaz
Adrián Merino-Salomón
Fabian Meyer
Michael Heymann
Germán Rivas
Marc Bramkamp
Petra Schwille
author_sort Diego A. Ramirez-Diaz
title FtsZ induces membrane deformations via torsional stress upon GTP hydrolysis
title_short FtsZ induces membrane deformations via torsional stress upon GTP hydrolysis
title_full FtsZ induces membrane deformations via torsional stress upon GTP hydrolysis
title_fullStr FtsZ induces membrane deformations via torsional stress upon GTP hydrolysis
title_full_unstemmed FtsZ induces membrane deformations via torsional stress upon GTP hydrolysis
title_sort ftsz induces membrane deformations via torsional stress upon gtp hydrolysis
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2021-06-01
description During bacterial cell division, the protein FtsZ is the main component of the contractile ring, though how precisely FtsZ treadmilling and its ability to deform membranes cooperate are unclear. Here, the authors show that dynamic FtsZ may deform lipid membranes via torsional stress that may provide sufficient force to constrict membranes in vivo and in vitro.
url https://doi.org/10.1038/s41467-021-23387-3
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