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

English version

Autoři: José E. Guzmán-Flores ^aff001; Lidia Steinemann-Hernández ^aff001; Luis E. González de la Vara ^aff002; Marina Gavilanes-Ruiz ^aff003; Tony Romeo ^aff004; Adrián F. Alvarez ^aff001; Dimitris Georgellis ^aff001
Působiště autorů: Departamento de Genética Molecular, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, México City, México ^aff001; Departamento de Biotecnología y Bioquímica, Unidad Irapuato, Cinvestav-IPN, Irapuato, Gto, México ^aff002; Departamento de Bioquímica, Facultad de Química, Universidad Nacional Autónoma de México, Mexico City, México ^aff003; Department of Microbiology and Cell Science, IFAS, University of Florida, Gainesville, Florida, United States of America ^aff004
Vyšlo v časopise: PLoS ONE 14(10)
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.pone.0223794

Souhrn

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.

Klíčová slova:

Lipids – Cell membranes – Membrane proteins – Outer membrane proteins – Lipoproteins – Signal peptides – Integral membrane proteins – Transmembrane transport proteins

Zdroje

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

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