The speed of FtsZ treadmilling is tightly regulated by membrane binding

Abstract As one of the key elements in bacterial cell division, the cytoskeletal protein FtsZ appears to be highly involved in circumferential treadmilling along the inner membrane, yielding circular vortices when transferred to flat membranes. However, it remains unclear how a membrane-targeted pro...

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Autores principales:	Daniela A. García-Soriano, Tamara Heermann, Ana Raso, Germán Rivas, Petra Schwille
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/8abeee3857ef495c848283c51c99a60d
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spelling	oai:doaj.org-article:8abeee3857ef495c848283c51c99a60d2021-12-02T17:45:21ZThe speed of FtsZ treadmilling is tightly regulated by membrane binding10.1038/s41598-020-67224-x2045-2322https://doaj.org/article/8abeee3857ef495c848283c51c99a60d2020-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-020-67224-xhttps://doaj.org/toc/2045-2322Abstract As one of the key elements in bacterial cell division, the cytoskeletal protein FtsZ appears to be highly involved in circumferential treadmilling along the inner membrane, yielding circular vortices when transferred to flat membranes. However, it remains unclear how a membrane-targeted protein can produce these dynamics. Here, we dissect the roles of membrane binding, GTPase activity, and the unstructured C-terminal linker on the treadmilling of a chimera FtsZ protein through in vitro reconstitution of different FtsZ-YFP-mts variants on supported membranes. In summary, our results suggest substantial robustness of dynamic vortex formation, where only significant mutations, resulting in abolished membrane binding or compromised lateral interactions, are detrimental for the generation of treadmilling rings. In addition to GTPase activity, which directly affects treadmilling dynamics, we found a striking correlation of membrane binding with treadmilling speed as a result of changing the MTS on our chimera proteins. This discovery leads to the hypothesis that the in vivo existence of two alternative tether proteins for FtsZ could be a mechanism for controlling FtsZ treadmilling.Daniela A. García-SorianoTamara HeermannAna RasoGermán RivasPetra SchwilleNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 10, Iss 1, Pp 1-9 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Daniela A. García-Soriano Tamara Heermann Ana Raso Germán Rivas Petra Schwille The speed of FtsZ treadmilling is tightly regulated by membrane binding
description	Abstract As one of the key elements in bacterial cell division, the cytoskeletal protein FtsZ appears to be highly involved in circumferential treadmilling along the inner membrane, yielding circular vortices when transferred to flat membranes. However, it remains unclear how a membrane-targeted protein can produce these dynamics. Here, we dissect the roles of membrane binding, GTPase activity, and the unstructured C-terminal linker on the treadmilling of a chimera FtsZ protein through in vitro reconstitution of different FtsZ-YFP-mts variants on supported membranes. In summary, our results suggest substantial robustness of dynamic vortex formation, where only significant mutations, resulting in abolished membrane binding or compromised lateral interactions, are detrimental for the generation of treadmilling rings. In addition to GTPase activity, which directly affects treadmilling dynamics, we found a striking correlation of membrane binding with treadmilling speed as a result of changing the MTS on our chimera proteins. This discovery leads to the hypothesis that the in vivo existence of two alternative tether proteins for FtsZ could be a mechanism for controlling FtsZ treadmilling.
format	article
author	Daniela A. García-Soriano Tamara Heermann Ana Raso Germán Rivas Petra Schwille
author_facet	Daniela A. García-Soriano Tamara Heermann Ana Raso Germán Rivas Petra Schwille
author_sort	Daniela A. García-Soriano
title	The speed of FtsZ treadmilling is tightly regulated by membrane binding
title_short	The speed of FtsZ treadmilling is tightly regulated by membrane binding
title_full	The speed of FtsZ treadmilling is tightly regulated by membrane binding
title_fullStr	The speed of FtsZ treadmilling is tightly regulated by membrane binding
title_full_unstemmed	The speed of FtsZ treadmilling is tightly regulated by membrane binding
title_sort	speed of ftsz treadmilling is tightly regulated by membrane binding
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/8abeee3857ef495c848283c51c99a60d
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The speed of FtsZ treadmilling is tightly regulated by membrane binding

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