The speed of FtsZ treadmilling is tightly regulated by membrane binding

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The speed of FtsZ treadmilling is tightly regulated by membrane binding. / García-Soriano, Daniela A.; Heermann, Tamara; Raso, Ana; Rivas, Germán; Schwille, Petra.

I: Scientific Reports, Bind 10, 10447, 06.2020.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

García-Soriano, DA, Heermann, T, Raso, A, Rivas, G & Schwille, P 2020, 'The speed of FtsZ treadmilling is tightly regulated by membrane binding', Scientific Reports, bind 10, 10447. https://doi.org/10.1038/s41598-020-67224-x

APA

García-Soriano, D. A., Heermann, T., Raso, A., Rivas, G., & Schwille, P. (2020). The speed of FtsZ treadmilling is tightly regulated by membrane binding. Scientific Reports, 10, [10447]. https://doi.org/10.1038/s41598-020-67224-x

CBE

García-Soriano DA, Heermann T, Raso A, Rivas G, Schwille P. 2020. The speed of FtsZ treadmilling is tightly regulated by membrane binding. Scientific Reports. 10:Article 10447. https://doi.org/10.1038/s41598-020-67224-x

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Author

García-Soriano, Daniela A. ; Heermann, Tamara ; Raso, Ana ; Rivas, Germán ; Schwille, Petra. / The speed of FtsZ treadmilling is tightly regulated by membrane binding. I: Scientific Reports. 2020 ; Bind 10.

Bibtex

@article{7c65ad4a480e486dad16233b8395d71f,
title = "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 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.",
author = "Garc{\'i}a-Soriano, {Daniela A.} and Tamara Heermann and Ana Raso and Germ{\'a}n Rivas and Petra Schwille",
year = "2020",
month = jun,
doi = "10.1038/s41598-020-67224-x",
language = "English",
volume = "10",
journal = "Scientific Reports",
issn = "2045-2322",
publisher = "Nature Publishing Group",

}

RIS

TY - JOUR

T1 - The speed of FtsZ treadmilling is tightly regulated by membrane binding

AU - García-Soriano, Daniela A.

AU - Heermann, Tamara

AU - Raso, Ana

AU - Rivas, Germán

AU - Schwille, Petra

PY - 2020/6

Y1 - 2020/6

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=85086852200&partnerID=8YFLogxK

U2 - 10.1038/s41598-020-67224-x

DO - 10.1038/s41598-020-67224-x

M3 - Journal article

C2 - 32591587

AN - SCOPUS:85086852200

VL - 10

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

M1 - 10447

ER -