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  • Title: Preferential insertion of lactose permease in phospholipid domains: AFM observations.
    Author: Picas L, Carretero-Genevrier A, Montero MT, Vázquez-Ibar JL, Seantier B, Milhiet PE, Hernández-Borrell J.
    Journal: Biochim Biophys Acta; 2010 May; 1798(5):1014-9. PubMed ID: 20096263.
    Abstract:
    We report the insertion of a transmembrane protein, lactose permease (LacY) from Escherichia coli (E. coli), in supported lipid bilayers (SLBs) of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine (POPE) and 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoglycerol (POPG), in biomimetic molar proportions. We provide evidence of the preferential insertion of LacY in the fluid domains. Analysis of the self-assembled protein arrangements showed that LacY: (i) is inserted as a monomer within fluid domains of SLBs of POPE:POPG (3:1, mol/mol), (ii) has a diameter of approx. 7.8nm; and (iii) keeps an area of phospholipids surrounding the protein that is compatible with shells of phospholipids.
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