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. 2020 Jun 26;10:10447. doi: 10.1038/s41598-020-67224-x

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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FtsZ ring dynamics depends on three factors: membrane binding, lateral interactions and GTPase activity. GTPase activity¹² and strength of membrane binding will influence the ON (i) and OFF (iii) rates of FtsZ monomers or protofilament on the membrane. Once attached to the lipid interface (ii), lateral interactions will influence ring formation. The interplay of these three factors will determine the treadmilling speed of FtsZ-rings.