Lipid-protein interactions in Escherichia coli membranes overexpressing the sugar-H+ symporter, GalP EPR of spin-labelled lipids
作者： Anne Hubert , Peter J.F. Henderson , Derek Marsh
DOI: 10.1016/S0005-2736(03)00081-6
关键词: Chemistry 、 Population 、 Membrane lipids 、 Protein–lipid interaction 、 Cell membrane 、 Biochemistry 、 Membrane 、 GalP 、 Integral membrane protein 、 Phosphatidylethanolamine
摘要: The D-galactose-H(+) symport protein (GalP) of Escherichia coli is a homologue the human glucose transport protein, GLUT1. After amplified expression GalP transporter in E. coli, lipid-protein interactions were studied gradient-purified inner membranes by using spin-label electron paramagnetic resonance (EPR) spectroscopy. Phosphatidylethanolamine, -glycerol, -choline and -serine, addition to phosphatidic stearic acids, spin-labelled at 14 C-atom sn-2 chain. EPR spectra these spin labels probe amounts consist two components. One component corresponds lipid population whose motion restricted direct interaction with transmembrane sections integral protein. other greater chain mobility, similar single-component spectrum lipids extract. Quantitation protein-interacting allows determination stoichiometry selectivity interactions. On average, approximately 20 mol are motionally per 52 kDa membranes. At pH assay, there relatively little between different phospholipids tested. Only acid displays stronger preferential this
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