Active membrane viscoelasticity by the bacterial FtsZ-division protein

Langmuir : the ACS Journal of Surfaces and Colloids
Iván López-MonteroFrancisco Monroy

Abstract

At the early stages of the division process in Escherichia coli, the protein FtsZ forms a septal ring at the midcell. This Z-ring causes membrane constriction during bacterial division. The Z-ring associates to the lipid membrane through several membrane proteins, ZipA among them. Here, a simplified FtsZ-ZipA model was reconstituted onto Langmuir monolayers based in E. coli polar lipid extract. Brewster angle and atomic force microscopy have revealed membrane FtsZ-polymerization upon GTP hydrolysis. The compression viscoelasticity of these monolayers has been also investigated. The presence of protein induced softening and fluidization with respect to the bare lipid membrane. An active mechanism, based on the internal forces stressed by FtsZ filaments and transduced to the lipid membrane by ZipA, was suggested to underlie the observed behavior.

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Citations

Oct 17, 2012·Trends in Cell Biology·Ariadna MartosPetra Schwille
Aug 16, 2013·Molecular Microbiology·Sheng-Wen ChiuJudith P Armitage
Jun 27, 2014·Chemistry and Physics of Lipids·Pablo González de Prado SalasPedro Tarazona
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Jul 11, 2020·Advanced Biosystems·Daniel HürtgenPetra Schwille
Mar 1, 2019·Scientific Reports·Leonard M C SagisKarin Schroen
Jun 7, 2013·The Journal of Biological Chemistry·Ana Isabel RicoMiguel Vicente
Aug 4, 2020·The Cell Surface·Glauber R de S AraújoSusana Frases

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