Functional microdomains in bacterial membranes

López, Daniel; Kolter, Roberto

doi:10.1101/gad.1945010

Cited by 301 publications

(513 citation statements)

References 62 publications

(79 reference statements)

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“…Our findings imply a link between membrane order and protein function in prokaryotes. They also suggest a possible lipid target to address bacterial multidrug resistance, further implicating isoprenoidal lipid biosynthesis as a bacterial Achilles heel (25,26).…”

Section: Significancementioning

confidence: 99%

Hopanoids as functional analogues of cholesterol in bacterial membranes

Sáenz

Grosser

Bradley

et al. 2015

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

206

177

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The functionality of cellular membranes relies on the molecular order imparted by lipids. In eukaryotes, sterols such as cholesterol modulate membrane order, yet they are not typically found in prokaryotes. The structurally similar bacterial hopanoids exhibit similar ordering properties as sterols in vitro, but their exact physiological role in living bacteria is relatively uncharted. We present evidence that hopanoids interact with glycolipids in bacterial outer membranes to form a highly ordered bilayer in a manner analogous to the interaction of sterols with sphingolipids in eukaryotic plasma membranes. Furthermore, multidrug transport is impaired in a hopanoid-deficient mutant of the gram-negative Methylobacterium extorquens, which introduces a link between membrane order and an energy-dependent, membrane-associated function in prokaryotes. Thus, we reveal a convergence in the architecture of bacterial and eukaryotic membranes and implicate the biosynthetic pathways of hopanoids and other order-modulating lipids as potential targets to fight pathogenic multidrug resistance.

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Section: Significancementioning

confidence: 99%

Hopanoids as functional analogues of cholesterol in bacterial membranes

Sáenz

Grosser

Bradley

et al. 2015

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

206

177

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“…Many eukaryotic and prokaryotic proteins are known to require localization to lipid rafts in order to function correctly. 24,25 In addition, some proteins require a specific lipid content to be present in the membrane either to localize to this position or to function efficiently. 24,[26][27][28] For example, in S. aureus, loss of LysPG prevents localization of the CAMP-responsive two component sensing system SaeS and results in reduction in the overall levels of proteins involved in glycerolipid metabolism, cell wall metabolism and transportation.…”

Section: Loss Of Lyspgs Causes No Significant Effect On Protein Localmentioning

confidence: 99%

LysPGS formation inListeria monocytogeneshas broad roles in maintaining membrane integrity beyond antimicrobial peptide resistance

et al. 2014

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“…These experiments provide a quantitative measure of the relationship between cell curvature in bacteria, CL microdomain localization at the poles, and the positioning of amphiphilic, cytoplasmic proteins. Lipid microdomains in bacteria recently have been described as "lipid rafts" because they may have striking similarities to the structure and function of lipidordered domains in eukaryotic membranes (24,25).…”

mentioning

confidence: 99%

Cardiolipin microdomains localize to negatively curved regions of Escherichia coli membranes

Renner¹,

Weibel

2011

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

309

336

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Many proteins reside at the cell poles in rod-shaped bacteria. Several hypotheses have drawn a connection between protein localization and the large cell-wall curvature at the poles. One hypothesis has centered on the formation of microdomains of the lipid cardiolipin (CL), its localization to regions of high membrane curvature, and its interaction with membrane-associated proteins. A lack of experimental techniques has left this hypothesis unanswered. This paper describes a microtechnology-based technique for manipulating bacterial membrane curvature and quantitatively measuring its effect on the localization of CL and proteins in cells. We confined Escherichia coli spheroplasts in microchambers with defined shapes that were embossed into a layer of polymer and observed that the shape of the membrane deformed predictably to accommodate the walls of the microchambers. Combining this technique with epifluorescence microscopy and quantitative image analyses, we characterized the localization of CL microdomains in response to E. coli membrane curvature. CL microdomains localized to regions of high intrinsic negative curvature imposed by microchambers. We expressed a chimera of yellow fluorescent protein fused to the N-terminal region of MinD-a spatial determinant of E. coli division plane assembly-in spheroplasts and observed its colocalization with CL to regions of large, negative membrane curvature. Interestingly, the distribution of MinD was similar in spheroplasts derived from a CL synthase knockout strain. These studies demonstrate the curvature dependence of CL in membranes and test whether these structures participate in the localization of MinD to regions of negative curvature in cells.A central question in cell biology is how the spatial organization of proteins and lipids is established, maintained, and replicated and how it fluctuates in response to external stimuli. Eukaryotic cells use several mechanisms to accomplish this task, including a dynamic cytoskeleton that controls the spatial and temporal position of proteins, nucleic acid, and organelles (1). The formation of lipid microdomains in the membrane also is involved in the localization of integral membrane proteins (2). These mechanisms play a critical role in cell physiology and behavior.Bacteria also use mechanisms for controlling the intracellular location of proteins, lipids, and nucleic acid. The persistent historical view of bacterial cells as lacking spatial control over their intracellular components inhibited the field. Bacteria are sophisticated organisms that use tightly regulated physiological mechanisms similar to many of those used by eukaryotic cells, including controlling shape, regulating growth and division, transporting intracellular components (e.g., proteins, plasmids, DNA, and RNA), and polarizing the cell (3, 4). These organisms have several remarkable structural characteristics, but one of the most fundamental questions in this area of microbiology-how cells produce, maintain, and replicate their spatial organization-still...

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Functional microdomains in bacterial membranes

Cited by 301 publications

References 62 publications

Hopanoids as functional analogues of cholesterol in bacterial membranes

Hopanoids as functional analogues of cholesterol in bacterial membranes

LysPGS formation inListeria monocytogeneshas broad roles in maintaining membrane integrity beyond antimicrobial peptide resistance

Cardiolipin microdomains localize to negatively curved regions of Escherichia coli membranes

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