Proteomic analysis of Escherichia coli detergent-resistant membranes (DRM).
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 31603938.
- Also identified by DOI 10.1371/journal.pone.0223794 and PMC identifier 6788730.
- No licence information is recorded for this record.
- Because redistribution is not established, this page shows the abstract only. Follow the links below for the full text.
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.
Medical subject headings
- Escherichia coli
- Membrane Microdomains
- Membrane Proteins
- Proteomics