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Flotillin-mediated membrane fluidity controls peptidoglycan synthesis and MreB movement
Aleksandra Zielińska, Abigail Savietto, Anabela de Sousa Borges, Denis Martinez, Mélanie Berbon, Joël Roelofsen, Alwin Hartman, Rinse de Boer, Ida van der Klei, Anna Kh Hirsch, Birgit Habenstein, Marc Bramkamp, Dirk-Jan Scheffers

Flotillin-mediated membrane fluidity controls peptidoglycan synthesis and MreB movement

Science & Mathematics Published 2020 Verification Pending

Overview & Synopsis

The bacterial plasma membrane is an important cellular compartment. In recent years it has become obvious that protein complexes and lipids are not uniformly distributed within membranes. Current hypotheses suggest that flotillin proteins are required for the formation of complexes of membrane proteins including cell-wall synthetic proteins. We show here that bacterial flotillins are important factors for membrane fluidity homeostasis. Loss of flotillins leads to a decrease in membrane fluidity that in turn leads to alterations in MreB dynamics and, as a consequence, in peptidoglycan synthesis. These alterations are reverted when membrane fluidity is restored by a chemical fluidizer. In vitro, the addition of a flotillin increases membrane fluidity of liposomes. Our data support a model in which flotillins are required for direct control of membrane fluidity rather than for the formation of protein complexes via direct protein-protein interactions.

Indexed from repository: HAL Open Science (hal.science)
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Document Information

Document Title Flotillin-mediated membrane fluidity controls peptidoglycan synthesis and MreB movement
Author / Organization Aleksandra Zielińska, Abigail Savietto, Anabela de Sousa Borges, Denis Martinez, Mélanie Berbon, Joël Roelofsen, Alwin Hartman, Rinse de Boer, Ida van der Klei, Anna Kh Hirsch, Birgit Habenstein, Marc Bramkamp, Dirk-Jan Scheffers
Subject & Discipline Multidisciplinary Academic Open Research
Categories Science & Mathematics
Publication Year 2020
License / Rights Open Access / Creative Commons
Resource Verification Listed PDF (Verification Pending)
Original Host Website HAL Open Science (hal.science)
File Format application/pdf (Portable Document Format)
Language EN
Catalog ID DOC-198284
Original Source Link Visit Source Page on hal.science »