Next Article in Journal
An Empirical Analysis of the Perceived Challenges and Benefits of Introducing Biosimilars in Bangladesh: A Paradigm Shift
Next Article in Special Issue
Numerical Simulation and FRAP Experiments Show That the Plasma Membrane Binding Protein PH-EFA6 Does Not Exhibit Anomalous Subdiffusion in Cells
Previous Article in Journal
Assessment of the Quorum Sensing Inhibition Activity of a Non-Toxic Chitosan in an N-Acyl Homoserine Lactone (AHL)-Based Escherichia coli Biosensor
Previous Article in Special Issue
The Many Faces of Amphipathic Helices
Article Menu

Export Article

Open AccessReview
Biomolecules 2018, 8(3), 88; https://doi.org/10.3390/biom8030088

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

1
Institute for Integrative Biology of the Cell (I2BC), CEA/Institut des Sciences du Vivant Fréderic-Joliot/SB2SM, CNRS UMR 9198, Université Paris-Sud, Université Paris-Saclay, 91191 Gif sur Yvette CEDEX, France
2
Institut FEMTO-ST, UMR CNRS 6174, Université Bourgogne Franche-Comté, 15B avenue des Montboucons, 25030 Besançon CEDEX, France
*
Authors to whom correspondence should be addressed.
Received: 30 July 2018 / Revised: 31 August 2018 / Accepted: 31 August 2018 / Published: 4 September 2018
(This article belongs to the Special Issue Cellular Membrane Domains and Organization)
Full-Text   |   PDF [880 KB, uploaded 4 September 2018]   |  

Abstract

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. View Full-Text
Keywords: intracellular membranes; Escherichia coli; membrane domains; vesicles; tubules; membrane curvature; membrane protein overexpression intracellular membranes; Escherichia coli; membrane domains; vesicles; tubules; membrane curvature; membrane protein overexpression
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).
SciFeed

Share & Cite This Article

MDPI and ACS Style

Jamin, N.; Garrigos, M.; Jaxel, C.; Frelet-Barrand, A.; Orlowski, S. Ectopic Neo-Formed Intracellular Membranes in Escherichia coli: A Response to Membrane Protein-Induced Stress Involving Membrane Curvature and Domains. Biomolecules 2018, 8, 88.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Biomolecules EISSN 2218-273X Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top