title: Cardiolipin interaction with subunit c of ATP synthase: solid-state NMR characterization.
abstract: The interaction of lipids with subunit c from F1F0 ATP synthase is studied by biophysical methods. Subunit c from both Escherichia coli and Streptococcus pneumoniae interacts and copurifies with cardiolipin. Solid state NMR data on oligomeric rings of F0 show that the cardiolipin interacts with the c subunit in membrane bilayers. These studies offer strong support for the hypothesis that F0 has specific interactions with cardiolipin.
authors.affiliation: Department of Chemistry, Columbia University, 3000 Broadway, New York, NY 10027, United States.
authors.forename: Ségolène
authors.initials: S
authors.lastname: Laage
authors.affiliation: Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Ave., Bronx, NY 10461, United States.
authors.forename: Yisong
authors.initials: Y
authors.lastname: Tao
authors.affiliation: Department of Chemistry, Columbia University, 3000 Broadway, New York, NY 10027, United States. Electronic address: aem5@columbia.edu.
authors.forename: Ann E
authors.initials: AE
authors.lastname: McDermott
mesh_terms: D002308:Cardiolipins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D025261:Mitochondrial Proton-Translocating ATPases / Q000737:chemistry*; D021122:Protein Subunits
chemical_list: D002308:Cardiolipins; D021122:Protein Subunits; C474451:F1F0-ATP synthase; D025261:Mitochondrial Proton-Translocating ATPases
keywords: ATP synthase; Cardiolipin; Lipid-protein interaction; Solid-state NMR