Flotillin mediated membrane fluidity controls peptidoglycan synthesis and MreB movement

Zielińska, Aleksandra; Savietto, Abigail; Borges, Anabela; Roelofsen, Joël R; Hartman, Alwin M.; Boer, Rinse de; Klei, Ida J. van der; Hirsch, Anna K. H.; Bramkamp, Marc; Scheffers, Dirk‐Jan

doi:10.1101/736819

Cited by 13 publications

(21 citation statements)

References 66 publications

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“…Inositol acylation is triggered by membrane fluidizing chemicals. Benzyl alcohol is a membranefluidizing chemical extensively used for both eukaryotic and prokaryotic membranes (26)(27)(28)(29)(30)(31)(32)(33)(34)(35)(36), and we have previously shown that benzyl alcohol disrupts membrane domain organization in M. smegmatis (21).…”

Section: Resultsmentioning

confidence: 99%

Inositol acylation of phosphatidylinositol mannosides: a rapid mass response to membrane fluidization in mycobacteria

Nguyen

Kado²,

Prithviraj³

et al. 2022

Journal of Lipid Research

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Section: Resultsmentioning

confidence: 99%

Inositol acylation of phosphatidylinositol mannosides: a rapid mass response to membrane fluidization in mycobacteria

Nguyen

Kado²,

Prithviraj³

et al. 2022

Journal of Lipid Research

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“…The influence of other factors related to the physico-chemical properties of the lipid bilayer, such as membrane fluidity, on the lateral mobility of FloA and FloT assemblies were also evaluated. Flotillins have been suggested to influence membrane fluidity 27,63 . It might therefore be that membrane fluidity regulates the lateral mobility of FloA and FloT assemblies.…”

Section: Resultsmentioning

confidence: 99%

The Bacterial Cytoskeleton Spatially Confines Functional Membrane Microdomains

Machta

et al. 2020

Preprint

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22Cell membranes laterally segregate into microdomains enriched in certain lipids and scaffold 23 proteins. Membrane microdomains modulate protein-protein interactions and are essential for cell 24 polarity, signaling and membrane trafficking. How cells organize their membrane microdomains, and 25 the physiological importance of these microdomains, is unknown. In eukaryotes, the cortical actin 26 cytoskeleton is proposed to act like a fence, constraining the dynamics of membrane microdomains. 27Like their eukaryotic counterparts, bacterial cells have functional membrane microdomains (FMMs) 28 that act as platforms for the efficient oligomerization of protein complexes. In this work, we used the 29 model organism Bacillus subtilis to demonstrate that FMM organization and movement depend 30 primarily on the interaction of FMM scaffold proteins with the domains' protein cargo, rather than with 31 domain lipids. Additionally, the MreB actin-like cytoskeletal network that underlies the bacterial 32 membrane was found to frame areas of the membrane in which FMM mobility is concentrated. 33Variations in membrane fluidity did not affect FMM mobility whereas alterations in cell wall organization 34 affected FMM mobility substantially. Interference with MreB organization alleviates FMM spatial 35 confinement whereas, by contrast, inhibition of cell wall synthesis strengthens FMM confinement. The 36 restriction of FMM lateral mobility by the submembranous actin-like cytoskeleton or the extracellular 37 wall cytoskeleton appears to be a conserved mechanism in prokaryotic and eukaryotic cells for 38 localizing functional protein complexes in specific membrane regions, thus contributing to the 39 organization of cellular processes. 40 41 42 43 48 actually heterogeneous fluids, with different membrane lipid species laterally segregating into sub-49 micrometer domains, driven by their physico-chemical properties 2-4 . This heterogeneous organization 50 of membrane lipids leads to a heterogeneous distribution of the embedded membrane proteins, which 51 appears essential for their functionality 5 . Membrane microdomains are widely present, mobile 52 structures that vary in size from transient protein clusters measured in nm 6 to large micron-sized stable 53 domains such as desmosomes 7 . These domains harbor proteins specialized in membrane trafficking, 54 cell-cell adhesion, and signal transduction, and they provide targets for viral entry 8 . 56It is now appreciated that membrane proteins can significantly impact membrane organization, in 57 particular stabilizing membrane domains. For instance, the scaffold activity of the flotillin proteins FLO1 58 and FLO2 plays an important role in stabilizing some eukaryotic membrane rafts ("lipid rafts") 9-11 ; it 59 would seem that this raft organization occurs in part through the capture and stabilization of specific 60 lipids by flotillins 12,13 . In addition, the activity of the flotillin scaffold contributes to the recruitment of 61 other raft-associated proteins, thus facilitatin...

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“…The copyright holder for this preprint this version posted December 4, 2022. ; https://doi.org/10.1101/2022.12.03.519008 doi: bioRxiv preprint properties. Membrane fluidity is important for elongasome-dependent PG-synthesis (51)(52)(53), and the fapR* allele increases sensitivity to both detergents and temperature. These phenotypes are suggestive of a possible fluidizing effect on the membrane.…”

Section: Discussionmentioning

confidence: 99%

“…Our phenotypic analysis suggests that the fapR* allele may also alter membrane 16 properties. Membrane fluidity is important for elongasome-dependent PG-synthesis (51)(52)(53), and the fapR* allele increases sensitivity to both detergents and temperature. These phenotypes are suggestive of a possible fluidizing effect on the membrane.…”

Section: Discussionmentioning

confidence: 99%

A decrease in fatty acid synthesis rescues cells with limited peptidoglycan synthesis capacity

Willdigg

Helmann

2022

Preprint

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Proper synthesis and maintenance of a multilayered cell envelope is critical for bacterial fitness. However, whether genetic mechanisms exist to coordinate synthesis of the membrane and peptidoglycan envelope layers is unclear. InBacillus subtilis, synthesis of peptidoglycan (PG) during cell elongation is mediated by an elongasome complex acting in concert with class A PBPs (aPBPs). We previously described mutant strains limited in their capacity for PG synthesis due to a loss of aPBPs and an inability to upregulate elongasome function. Growth of these PG-limited cells can be restored by suppressor mutations predicted to decrease membrane synthesis. One suppressor mutation leads to an altered function repressor, FapR*, that functions as a super-repressor and leads to decreased transcription of fatty acid synthesis genes. Consistent with fatty acid limitation mitigating cell wall homeostasis defects, inhibition of FAS by cerulenin also restored growth of PG-limited cells. Moreover, cerulenin rescued the growth of wild-type (WT) cells in the presence of otherwise inhibitory concentrations of β-lactams. These results imply that limiting PG synthesis results in impaired growth, in part, due to an imbalance of PG and cell membrane synthesis and thatB. subtilislacks a robust genetic mechanism to coordinate the balanced synthesis of these two envelope layers.

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Flotillin mediated membrane fluidity controls peptidoglycan synthesis and MreB movement

Cited by 13 publications

References 66 publications

Inositol acylation of phosphatidylinositol mannosides: a rapid mass response to membrane fluidization in mycobacteria

Inositol acylation of phosphatidylinositol mannosides: a rapid mass response to membrane fluidization in mycobacteria

The Bacterial Cytoskeleton Spatially Confines Functional Membrane Microdomains

A decrease in fatty acid synthesis rescues cells with limited peptidoglycan synthesis capacity

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