Preferential insertion of lactose permease in phospholipid domains: AFM observations

被引：17
作者：
Picas, Laura [1 ]
Carretero-Genevrier, Adrian [5 ]
Teresa Montero, M. [1 ,2 ]
Vazquez-Ibar, J. L. [3 ,4 ]
Seantier, Bastien [6 ]
Milhiet, Pierre-Emmanuel [6 ]
Hernandez-Borrell, Jordi [1 ,2 ]
机构：
[1] Univ Barcelona, Fac Farm, Dept Fisicoquim, E-08028 Barcelona, Spain
[2] Univ Barcelona, Inst Nanociencia & Nanotecnol, E-08028 Barcelona, Spain
[3] ICREA, Barcelona 08028, Spain
[4] Inst Recerca Biomed, Barcelona 08028, Spain
[5] CSIC, ICMAB, Bellaterra 08193, Spain
[6] Univ Montpellier, CNRS, UMR 5048, Ctr Biochim Struct, F-34059 Montpellier, France
来源：
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2010年 / 1798卷 / 05期
关键词：
Lactose permease; AFM; Phospholipid domains; ESCHERICHIA-COLI; MEMBRANE-PROTEINS; LIPID-BILAYER; CONFORMATIONAL FLEXIBILITY; FORCE MICROSCOPY; CRYSTALLIZATION; TRANSPORT; LIPOSOMES; CALCIUM;
D O I：
10.1016/j.bbamem.2010.01.008
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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 1palmitoy1-2-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. 7.8 nm; and (iii) keeps an area of phospholipids surrounding the protein that is compatible with shells of phospholipids. (C) 2010 Elsevier B.V. All rights reserved.
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收藏
页码：1014 / 1019
页数：6
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