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Proteomic analysis of Escherichia coli detergent-resistant membranes (DRM).
Guzmán-Flores, José E; Steinemann-Hernández, Lidia; González de la Vara, Luis E; Gavilanes-Ruiz, Marina; Romeo, Tony; Alvarez, Adrián F; Georgellis, Dimitris.
Afiliación
  • Guzmán-Flores JE; Departamento de Genética Molecular, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, México City, México.
  • Steinemann-Hernández L; Departamento de Genética Molecular, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, México City, México.
  • González de la Vara LE; Departamento de Biotecnología y Bioquímica, Unidad Irapuato, Cinvestav-IPN, Irapuato, Gto, México.
  • Gavilanes-Ruiz M; Departamento de Bioquímica, Facultad de Química, Universidad Nacional Autónoma de México, Mexico City, México.
  • Romeo T; Department of Microbiology and Cell Science, IFAS, University of Florida, Gainesville, Florida, United States of America.
  • Alvarez AF; Departamento de Genética Molecular, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, México City, México.
  • Georgellis D; Departamento de Genética Molecular, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, México City, México.
PLoS One ; 14(10): e0223794, 2019.
Article en En | MEDLINE | ID: mdl-31603938
ABSTRACT
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.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Contexto en salud: 3_ND Problema de salud: 3_neglected_diseases / 3_zoonosis Asunto principal: Microdominios de Membrana / Proteómica / Escherichia coli / Proteínas de la Membrana Idioma: En Revista: PLoS One Asunto de la revista: CIENCIA / MEDICINA Año: 2019 Tipo del documento: Article

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Contexto en salud: 3_ND Problema de salud: 3_neglected_diseases / 3_zoonosis Asunto principal: Microdominios de Membrana / Proteómica / Escherichia coli / Proteínas de la Membrana Idioma: En Revista: PLoS One Asunto de la revista: CIENCIA / MEDICINA Año: 2019 Tipo del documento: Article
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