Proteomic analysis of Escherichia coli detergent-resistant membranes (DRM).

Membrane microdomains or lipid rafts compartmentalize cellular processes by laterally organizing membrane components. Such sub-membrane structures were mainly described in eukaryotic cells, but, recently, also in bacteria. Here, the protein content of lipid rafts in Escherichia coli was explored by...

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Main Authors: José E Guzmán-Flores, Lidia Steinemann-Hernández, Luis E González de la Vara, Marina Gavilanes-Ruiz, Tony Romeo, Adrián F Alvarez, Dimitris Georgellis
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2019-01-01
Series:PLoS ONE
Online Access:https://doi.org/10.1371/journal.pone.0223794
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spelling doaj-9e9bfe44b9a64bba93296f1317f155f62021-03-03T21:09:56ZengPublic Library of Science (PLoS)PLoS ONE1932-62032019-01-011410e022379410.1371/journal.pone.0223794Proteomic analysis of Escherichia coli detergent-resistant membranes (DRM).José E Guzmán-FloresLidia Steinemann-HernándezLuis E González de la VaraMarina Gavilanes-RuizTony RomeoAdrián F AlvarezDimitris GeorgellisMembrane microdomains or lipid rafts compartmentalize cellular processes by laterally organizing membrane components. Such sub-membrane structures were mainly described in eukaryotic cells, but, recently, also in bacteria. Here, the protein content of lipid rafts in Escherichia coli was explored by mass spectrometry analyses of Detergent Resistant Membranes (DRM). We report that at least three of the four E. coli flotillin homologous proteins were found to reside in DRM, along with 77 more proteins. Moreover, the proteomic data were validated by subcellular localization, using immunoblot assays and fluorescence microscopy of selected proteins. Our results confirm the existence of lipid raft-like microdomains in the inner membrane of E. coli and represent the first comprehensive profiling of proteins in these bacterial membrane platforms.https://doi.org/10.1371/journal.pone.0223794
collection DOAJ
language English
format Article
sources DOAJ
author José E Guzmán-Flores
Lidia Steinemann-Hernández
Luis E González de la Vara
Marina Gavilanes-Ruiz
Tony Romeo
Adrián F Alvarez
Dimitris Georgellis
spellingShingle José E Guzmán-Flores
Lidia Steinemann-Hernández
Luis E González de la Vara
Marina Gavilanes-Ruiz
Tony Romeo
Adrián F Alvarez
Dimitris Georgellis
Proteomic analysis of Escherichia coli detergent-resistant membranes (DRM).
PLoS ONE
author_facet José E Guzmán-Flores
Lidia Steinemann-Hernández
Luis E González de la Vara
Marina Gavilanes-Ruiz
Tony Romeo
Adrián F Alvarez
Dimitris Georgellis
author_sort José E Guzmán-Flores
title Proteomic analysis of Escherichia coli detergent-resistant membranes (DRM).
title_short Proteomic analysis of Escherichia coli detergent-resistant membranes (DRM).
title_full Proteomic analysis of Escherichia coli detergent-resistant membranes (DRM).
title_fullStr Proteomic analysis of Escherichia coli detergent-resistant membranes (DRM).
title_full_unstemmed Proteomic analysis of Escherichia coli detergent-resistant membranes (DRM).
title_sort proteomic analysis of escherichia coli detergent-resistant membranes (drm).
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2019-01-01
description Membrane microdomains or lipid rafts compartmentalize cellular processes by laterally organizing membrane components. Such sub-membrane structures were mainly described in eukaryotic cells, but, recently, also in bacteria. Here, the protein content of lipid rafts in Escherichia coli was explored by mass spectrometry analyses of Detergent Resistant Membranes (DRM). We report that at least three of the four E. coli flotillin homologous proteins were found to reside in DRM, along with 77 more proteins. Moreover, the proteomic data were validated by subcellular localization, using immunoblot assays and fluorescence microscopy of selected proteins. Our results confirm the existence of lipid raft-like microdomains in the inner membrane of E. coli and represent the first comprehensive profiling of proteins in these bacterial membrane platforms.
url https://doi.org/10.1371/journal.pone.0223794
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