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Ectopic Neo-Formed Intracellular Membranes in Escherichia coli: A Response to Membrane Protein-Induced Stress Involving Membrane Curvature and Domains

期刊

BIOMOLECULES
卷 8, 期 3, 页码 -

出版社

MDPI
DOI: 10.3390/biom8030088

关键词

intracellular membranes; Escherichia coli; membrane domains; vesicles; tubules; membrane curvature; membrane protein overexpression

资金

  1. CEA (Commissariat a l'energie atomique et aux energies alternatives)
  2. CNRS (Centre National de la Recherche Scientifique)
  3. University Paris South
  4. French National Research Agency [ANR-17-CE11-015-01]

向作者/读者索取更多资源

Bacterial cytoplasmic membrane stress induced by the overexpression of membrane proteins at high levels can lead to formation of ectopic intracellular membranes. In this review, we report the various observations of such membranes in Escherichia coli, compare their morphological and biochemical characterizations, and we analyze the underlying molecular processes leading to their formation. Actually, these membranes display either vesicular or tubular structures, are separated or connected to the cytoplasmic membrane, present mono- or polydispersed sizes and shapes, and possess ordered or disordered arrangements. Moreover, their composition differs from that of the cytoplasmic membrane, with high amounts of the overexpressed membrane protein and altered lipid-to-protein ratio and cardiolipin content. These data reveal the importance of membrane domains, based on local specific lipid-protein and protein-protein interactions, with both being crucial for local membrane curvature generation, and they highlight the strong influence of protein structure. Indeed, whether the cylindrically or spherically curvature-active proteins are actively curvogenic or passively curvophilic, the underlying molecular scenarios are different and can be correlated with the morphological features of the neo-formed internal membranes. Delineating these molecular mechanisms is highly desirable for a better understanding of protein-lipid interactions within membrane domains, and for optimization of high-level membrane protein production in E. coli.

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