MinD and MinE Interact with Anionic Phospholipids and Regulate Division Plane Formation in Escherichia coli

Renner, Lars D.; Weibel, Douglas B.

doi:10.1074/jbc.m112.407817

Cited by 82 publications

(105 citation statements)

References 49 publications

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“…The existence of cardiolipin domains could further explain why the effect is specific to bacterial over mammalian membranes. In fact, bacterial membranes (i) are more negatively charged than eukaryotic membranes; (ii) contain a higher proportion of negative intrinsic curvature lipids, where proteins involved in the formation of the division plane are located (78,79); and (iii) exhibit a dilational elasticity modulus that is much lower than the one found in mammalian membranes (80).…”

Section: Discussionmentioning

confidence: 98%

Negatively Charged Lipids as a Potential Target for New Amphiphilic Aminoglycoside Antibiotics

Sautrey¹,

Khoury²,

Santos³

et al. 2016

Journal of Biological Chemistry

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Bacterial membranes are highly organized, containing specific microdomains that facilitate distinct protein and lipid assemblies. Evidence suggests that cardiolipin molecules segregate into such microdomains, probably conferring a negative curvature to the inner plasma membrane during membrane fission upon cell division. 3,6-Dinonyl neamine is an amphiphilic aminoglycoside derivative active against Pseudomonas aeruginosa, including strains resistant to colistin. The mechanisms involved at the molecular level were identified using lipid models (large unilamellar vesicles, giant unilamelllar vesicles, and lipid monolayers) that mimic the inner membrane of P. aeruginosa. The study demonstrated the interaction of 3,6-dinonyl neamine with cardiolipin and phosphatidylglycerol, two negatively charged lipids from inner bacterial membranes. This interaction induced membrane permeabilization and depolarization. Lateral segregation of cardiolipin and membrane hemifusion would be critical for explaining the effects induced on lipid membranes by amphiphilic aminoglycoside antibiotics. The findings contribute to an improved understanding of how amphiphilic aminoglycoside antibiotics that bind to negatively charged lipids like cardiolipin could be promising antibacterial compounds.

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Section: Discussionmentioning

confidence: 98%

Negatively Charged Lipids as a Potential Target for New Amphiphilic Aminoglycoside Antibiotics

Sautrey¹,

Khoury²,

Santos³

et al. 2016

Journal of Biological Chemistry

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“…Considerable evidence suggests that CL molecules form membrane microdomains that may confer negative curvature to the inner plasma membrane during membrane fission for cell division and sporulation processes (28)(29)(30)(31). It is tempting to speculate that modified lipid A structures require specific increases in CL to maintain proper membrane curvature during bacterial replication.…”

Section: Discussionmentioning

confidence: 99%

PhoPQ regulates acidic glycerophospholipid content of the Salmonella Typhimurium outer membrane

Dalebroux¹,

Matamouros²,

Whittington

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

139

172

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Significance The outer membrane (OM) of Gram-negative bacteria is composed of lipopolysaccharide (LPS) and glycerophospholipids (GPLs). Environmental regulation of LPS promotes bacterial resistance to host cationic antimicrobial peptides by altering surface charge and hydrophobicity. This work demonstrates that pathogenic Salmonella coordinately regulate GPL and LPS through the PhoPQ regulatory proteins and the OM palmitoyltransferase enzyme PagP. The broad conservation of PhoPQ and PagP in bacteria suggests that environmental regulation of OM GPL may be a conserved stress-response strategy for antimicrobial resistance. Improved understanding of OM GPL synthesis, transport, and modification could lead to new therapies that target the bacterial OM barrier.

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“…It would be interesting to see whether the polar enrichments of lipids and proteins are also correlated at the single-cell level. This phenomenon is not unique: other proteins might also exploit the particular lipid content at the poles for their local accumulation (Renner and Weibel, 2012).…”

Section: Self-assembly and Nucleoid Occlusionmentioning

confidence: 99%

“…1D). For example, some proteins interact preferentially with specific phospholipids such as cardiolipin (Mileykovskaya et al, 2003;Renner and Weibel, 2012) that are enriched in the cytoplasmic membrane surrounding the poles of several bacterial species (Mileykovskaya and Dowhan, 2000;Kawai et al, 2004;Bernal et al, 2007). The polar enrichment of cardiolipin is driven by its intrinsic curvature, which thermodynamically favors its insertion as clusters ('microdomains') in highly negatively curved membranes (Huang et al, 2006;Mukhopadhyay et al, 2008;Renner and Weibel, 2011).…”

Section: Self-assembly and Nucleoid Occlusionmentioning

confidence: 99%

How do bacteria localize proteins to the cell pole?

Laloux

Jacobs‐Wagner

2014

Journal of Cell Science

158

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It is now well appreciated that bacterial cells are highly organized, which is far from the initial concept that they are merely bags of randomly distributed macromolecules and chemicals. Central to their spatial organization is the precise positioning of certain proteins in subcellular domains of the cell. In particular, the cell poles -the ends of rod-shaped cells -constitute important platforms for cellular regulation that underlie processes as essential as cell cycle progression, cellular differentiation, virulence, chemotaxis and growth of appendages. Thus, understanding how the polar localization of specific proteins is achieved and regulated is a crucial question in bacterial cell biology. Often, polarly localized proteins are recruited to the poles through their interaction with other proteins or protein complexes that were already located there, in a so-called diffusion-and-capture mechanism. Bacteria are also starting to reveal their secrets on how the initial pole 'recognition' can occur and how this event can be regulated to generate dynamic, reproducible patterns in time (for example, during the cell cycle) and space (for example, at a specific cell pole). Here, we review the major mechanisms that have been described in the literature, with an emphasis on the self-organizing principles. We also present regulation strategies adopted by bacterial cells to obtain complex spatiotemporal patterns of protein localization.

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MinD and MinE Interact with Anionic Phospholipids and Regulate Division Plane Formation in Escherichia coli

Cited by 82 publications

References 49 publications

Negatively Charged Lipids as a Potential Target for New Amphiphilic Aminoglycoside Antibiotics

Negatively Charged Lipids as a Potential Target for New Amphiphilic Aminoglycoside Antibiotics

PhoPQ regulates acidic glycerophospholipid content of the Salmonella Typhimurium outer membrane

How do bacteria localize proteins to the cell pole?

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