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Picas, L, Carretero-Genevrier, A, Montero, MT, Vázquez-Ibar, JL, Seantier, B, Milhiet, PE and Hernández-Borrell, J (2010) Preferential insertion of lactose permease in phospholipid domains: AFM observations. Biochim. Biophys. Acta 1798:1014-9


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.


PubMed Online version:10.1016/j.bbamem.2010.01.008


Escherichia coli/enzymology; Lipid Bilayers/chemistry; Membrane Transport Proteins/chemistry; Microscopy, Atomic Force; Phosphatidylethanolamines/chemistry; Phosphatidylglycerols/chemistry; Phospholipids/chemistry


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